Binding Site Information of Target
Target General Information | Top | ||||
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Target ID | T53159 | Target Info | |||
Target Name | ERK activator kinase 7 (MAP2K7) | ||||
Synonyms | Stress-activated protein kinase kinase 4; SKK4; SAPKK4; SAPKK-4; SAPK kinase 4; PRKMK7; Mitogen-activated protein kinase kinase 7; MKK7; MEK7; MEK 7; MAPKK 7; MAPK/ERK kinase7; MAPK/ERK kinase 7; MAP kinase kinase 7; JNKK2; JNKK 2; JNK-activating kinase 2; JNK kinase 2; JNK activating kinase 2; Dual specificity mitogen-activated protein kinase kinase 7; C-Jun N-terminal kinase kinase 2 | ||||
Target Type | Literature-reported Target | ||||
Gene Name | MAP2K7 | ||||
Biochemical Class | Kinase | ||||
UniProt ID |
Drug Binding Sites of Target | Top | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Ligand Name: Ibrutinib | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) with ibrutinib bound at allosteric site | PDB:6YZ4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
KQTGYLTIGG
126 QRYQAEINDL136 ENLGEMGGQV150 WKMRFRKTGH160 VIAVKQMRRS170 GNKEENKRIL 180 MDLDVVLKSH190 DCPYIVQCFG200 TFITNTDVFI210 AMELMGTCAE220 KLKKRMQGPI 230 PERILGKMTV240 AIVKALYYLK250 EKHGVIHRDV260 KPSNILLDER270 GQIKLCDFGI 280 SGRLGCAAYM300 APERIDPPDP310 TKPDYDIRAD320 VWSLGISLVE330 LATGQFPYKN 340 CKTDFEVLTK350 VLQEEPPLLP360 GHMGFSGDFQ370 SFVKDCLTKD380 HRKRPKYNKL 390 LEHSFIKRYE400 TLEVDVASWF410 KDVMAKTESP420
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☰Loading data... Dynamically generated for selected residues. Nodes can be dragged or clicked. Label: Selection: Name:
PDB ID: Option 1, search with your selection (all residues are selected by default) in the loaded structures: Option 2, search with PDB ID and chain name: PDB ID: Chain Name: Option 3, search with a PDB file: Foldseek web server. 1. your selection (all residues are selected by default) in the loaded structures to 2 (Optional). Once you see the structure neighbors, you can view the alignment in iCn3D by inputing a list of PDB chain IDs or AlphaFold UniProt IDs below. The PDB chain IDs are the same as the record names such as "1HHO_A". The UniProt ID is the text between "AF-" and "-F1". For example, the UniProt ID for the record name "AF-P69905-F1-model_v4" is "P69905". Chain ID List: BCIF/MMTF ID: PDB ID: Very high (pLDDT > 90) Confident (90 > pLDDT > 70) Low (70 > pLDDT > 50) Very low (pLDDT < 50) AlphaFold Uniprot ID: PAE Map: NCBI Protein Accession: PDB File: Multiple PDB Files: The custom JSON file on residue colors has the following format for proteins("ALA" and "ARG") and nucleotides("G" and "A"): {"ALA":"#C8C8C8", "ARG":"#145AFF", ..., "G":"#008000", "A":"#6080FF", ...} Residue Color File: The custom file for the structure has two columns separated by space or tab: residue number, and score in the range of 0-100. If you click "Apply Custom Color" button, the scores 0, 50 and 100 correspond to the three colors specified below. If you click "Apply Custom Tube", the selected residues will be displayed in a style similar to "B-factor Tube". Custom File: 1. Score to Color: 0: 50: 100: or 2. You can define your own reference numbers in a custom file using Excel, and then export it as a CSV file. An example file is shown below with cells separated by commas. refnum,11,12,,21,22,,10C,11C,20CThe first row defines the reference residue numbers, which could be any strings. The 1st cell could be anything. The rest cells are reference residue numbers (e.g., 11, 21, 10C, etc.) or empty cells. Each chain has a separate row. The first cell of the second row is the chain ID "1TUP_A". The rest cells are the corresponding real residue numbers for reference residue numbers in the first row. For example, the reference numbers for residues 100, 101, and 132 in the chain 1TUP_A are 11, 12, and 22, respectively. The fourth row shows another set of reference numners for the chain "1TUP_C". It could be a chain from a different structure. To select all residues corresponding to the reference numbers, you can simplay replace ":" with "%" in the Specification. For example, "%12" selects the residue 101 in 1TUP_A and the residue 111 in 1TUP_B. ".A%12" has the chain "A" filter and selects the residue 101 in 1TUP_A. Custom File: ID1: ID2: VAST+ based on VAST: VAST+ based on TM-align: All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: (Note: To align chains in custom PDB files, you could load them in "File > Open File > PDB Files (appendable)" and click "Analysis > Defined Sets". Finally select multiple chains in Defined Sets and click "File > Realign Selection".) All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: The sequence alignment (followed by structure alignment) is based on residue numbers in the First/Master chain: (Note: To align chains in custom PDB files, you could load them in "File > Open File > PDB Files (appendable)" and click "Analysis > Defined Sets". Finally select multiple chains in Defined Sets and click "File > Realign Selection".) All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: Each alignment is defined as " | "-separated residue lists in one line. "10-50" means a range of residues from 10 to 50. Option 1: Option 2: All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: Each alignment is defined as " | "-separated residue lists in one line. "10-50" means a range of residues from 10 to 50. Please specify the mutations with a comma separated mutation list. Each mutation can be specified as "[uppercase PDB ID or AlphaFold UniProt ID]_[Chain Name]_[Residue Number]_[One Letter Mutant Residue]". E.g., the mutation of N501Y in the E chain of PDB 6M0J can be specified as "6M0J_E_501_Y". For AlphaFold structures, the "Chain ID" is "A". If you load a custom structure without PDB or UniProt ID, you can open "Seq. & Annotations" window and find the chain ID such as "stru_A". The part before the underscore is the structure ID, which can be used to specify the mutation such as "stru_A_...". Remember to choose "Show Mutation in: Current Page". Mutations: ID Type: PDB IDAlphaFold UniProt ID Show Mutation in: Current PageNew Page Mol2 File: SDF File: XYZ File: URL in the same host: Multiple mmCIF Files: mmCIF ID: Note: The "biological unit" is the biochemically active form of a biomolecule, or Note: The "biological unit" is the biochemically active form of a biomolecule, BLAST search with the protein sequence ID or FASTA sequence as input. If the protein accession is not a PDB chain, the corresponding AlphaFold UniProt structure is used. Enter a protein sequence ID (or FASTA sequence) and the aligned protein accession, which can be found using the Protein Sequence ID(NCBI protein accession of a sequence): or FASTA sequence: Aligned Protein Accession (or a chain of a PDB): ESM Metagenomic Atlas. The sequence should be less than 400 characters. For any sequence longer than 400, please see the discussion here. The sequence to structure prediction is done via FASTA sequence: Protein/Gene name: PubChem CID/Name/InchI: Chemical SMILES: Share Link URL: Collection File: Structures: 2fofc contour at default threshold or at: σ fofc contour at default threshold or at: σ 2fofc contour at default threshold or at: σ URL in the same host: fofc contour at default threshold or at: σ URL in the same host: Custom Color: Grid Size: Salt Concentration: M Potential contour at: kT/e(25.6mV at 298K) Note: Only the selected residues are used for DelPhi potential calculation by solving linear Poisson-Boltzmann equation. Grid Size: Salt Concentration: M Surface with max potential at: kT/e(25.6mV at 298K) Surface: Opacity: Wireframe: Note: Only the selected residues are used for DelPhi potential calculation by solving linear Poisson-Boltzmann equation. Potential contour at: kT/e(25.6mV at 298K) Note: Always load a PDB file before loading a PQR or DelPhi potential file. Potential contour at: kT/e(25.6mV at 298K) Grid Size: Salt Concentration: M PQR URL in the same host: Phi URL in the same host: Cube URL in the same host: Note: Always load a PDB file before loading a PQR or DelPhi potential file. Symmetry: Distance: Contact Type:
4. Sort Interactions on: to show two lines of residue nodes to show map with atom details to show interactions with strength parameters in 0-200:
(Note: you can also adjust thresholds at #1 to add/remove interactions.) 5. and select new sets 1. Select sets below or use your current selection: 2. 1. Select sets below or use your current selection. 2. 1. Select sets below or use your current selection: 2. Overall maximum RMSD: Å 3. 1. Select sets below: 2. 1. Select sets below: 2. 1. Select sets below: 2. 1. Select sets below: 2. Hold Ctrl key to select multiple nodes/lines. Green: H-Bonds; Cyan: Salt Bridge/Ionic; Grey: Contacts Magenta: Halogen Bonds; Red: π-Cation; Blue: π-Stacking Scale: Hold Ctrl key to select multiple nodes. Scale: Note: Nodes/Residues can be dragged. Both nodes and dashed lines/interactions can be clicked to select residues. Color legend for interactions (dashed lines): Green: H-Bonds; Cyan: Salt Bridge/Ionic; Grey: Contacts Magenta: Halogen Bonds; Red: π-Cation; Blue: π-Stacking Scale: Hold Ctrl key to select multiple nodes. Scale: Hold Ctrl key to select multiple nodes. Scale:
Contour at: σ Contour at: σ Contour at: % of maximum EM values 1. Select the first set: 2. Sphere with a radius: Å 3. Select the second set to apply the sphere: 4. the sphere around the first set of atoms interacting/contacting residue pairs in a file 1. Extracellular membrane Z-axis position: Å 2. intracellular membrane Z-axis position: Å 3. the adjusted membranes 1. Z-axis position of the first X-Y plane: Å 2. Z-axis position of the second X-Y plane: Å 3. the region between the planes to Defined Sets 2. Size: 3. Color: 4. Pick TWO atoms while holding "Alt" key 5. 2. Size: 3. Color: 4. 1. Pick TWO atoms while holding "Alt" key 2. Line Color: 3. 1. Pick TWO atoms while holding "Alt" key 2. Color: 3. 1. Select two sets
3. 1. Select two sets
2. Line style: 3. Line radius: 4. Color: 5. Opacity: 6. 1. Select a set: 2. Shape: 3. Radius: 4. Color: 5. Opacity: 6. 1. Select sets for pairwise distances
Note: Each set is represented by a vector, which is the X-axis of the principle axes. The angles between the vectors are then calculated. 1. Select sets for pairwise angles
1. Pick TWO atoms while holding "Alt" key 2. Coil Radius: (for coils, default 0.3) Stick Radius: (for sticks, default 0.4) Cross-Linkage Radius: (for cross-linkages, default 0.4) Trace Radius: (for C alpha trace, O3' trace, default 0.4) Ribbon Thickness: (for helix and sheet ribbons, nucleotide ribbons, default 0.2) Protein Ribbon Width: (for helix and sheet ribbons, default 1.3) Nucleotide Ribbon Width: (for nucleotide ribbons, default 0.8) Ball Scale: (for styles 'Ball and Stick' and 'Dot', default 0.3) 1. Shininess: (for the shininess of the 3D objects, default 40) 2. Three directional lights: Key Light: (for the light strength of the key light, default 0.8) Fill Light: (for the light strength of the fill light, default 0.4) Back Light: (for the light strength of the back light, default 0.2) 3. Thickness: Line Radius: (for stabilizers, hydrogen bonds, distance lines, default 0.1) Coil Radius: (for coils, default 0.3) Stick Radius: (for sticks, default 0.4) Cross-Linkage Radius: (for cross-linkages, default 0.4) Trace Radius: (for C alpha trace, O3' trace, default 0.4) Ribbon Thickness: (for helix and sheet ribbons, nucleotide ribbons, default 0.2) Protein Ribbon Width: (for helix and sheet ribbons, default 1.3) Nucleotide Ribbon Width: (for nucleotide ribbons, default 0.8) Ball Scale: (for styles 'Ball and Stick' and 'Dot', default 0.3) 4. Show Glycan Cartoon: (0: hide, 1: show, default 0) 5. Show Membrane: (0: hide, 1: show, default 1) 6. Enlarge Command Window: (0: Regular, 1: Large, default 0) 1. URLs Used in Browsers Please copy one of the URLs below. They show the same result. (To add a title to share link, click "Windows > Your Note" and click "File > Share Link" again.) Original URL with commands: Lifelong Short URL:(To replace this URL, send a pull request to update share.html at iCn3D GitHub) Lifelong Short URL + Window Title:(To update the window title, click "Analysis > Your Note/Window Title".) 2. Commands Used in Jupyter Noteboook Please copy the following commands into a cell in Jupyter Notebook to show the same result. More details are at https://github.com/ncbi/icn3d/tree/master/jupyternotebook. Annotations:
Zoom: mouse wheel; Move: left button; Select Multiple Nodes: Ctrl Key and drag an Area Force on Nodes: Label Size: Internal Edges: Color each residue based on the percentage of solvent accessilbe surface area. The color ranges from blue, to white, to red for a percentage of 0, 35(variable), and 100, respectively. Middle Percentage(White): % Select residue based on the percentage of solvent accessilbe surface area. The values are in the range of 0-100. Min Percentage: % Max Percentage: % Select residue based on B-factor/pLDDT. The values are in the range of 0-100. Min B-factor/pLDDT: % Max B-factor/pLDDT: % X: Y: Z: Vector 2, X: Y: Z: The angle is: degree. 1: 5: 9: 13: 2: 6: 10: 14: 3: 7: 11: 15: Choose an Ig template for selected residues: Choose an Ig template to align with selected residues: |
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Click to View More Binding Site Information of This Target and Ligand Pair | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Ligand Name: 3-Sulfinoalanine | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) in complex with K00007 | PDB:6YG4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGQVWKM153 RFRKTGHVIA163 VKQMRRSGNK173 EENKRILMDL 183 DVVLKSHDCP193 YIVQCFGTFI203 TNTDVFIAME213 LMGTAEKLKK224 RMQGPIPERI 234 LGKMTVAIVK244 ALYYLKEKHG254 VIHRDVKPSN264 ILLDERGQIK274 LDFGISGIRA 319 DVWSLGISLV329 ELATGQFPYK339 NCKTDFEVLT349 KVLQEEPPLL359 PGHMGFSGDF 369 QSFVKDCLTK379 DHRKRPKYNK389 LLEHSFIKRY399 ETLEVDVASW409 FKDVMAKT |
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☰Loading data... Dynamically generated for selected residues. Nodes can be dragged or clicked. Label: Selection: Name:
PDB ID: Option 1, search with your selection (all residues are selected by default) in the loaded structures: Option 2, search with PDB ID and chain name: PDB ID: Chain Name: Option 3, search with a PDB file: Foldseek web server. 1. your selection (all residues are selected by default) in the loaded structures to 2 (Optional). Once you see the structure neighbors, you can view the alignment in iCn3D by inputing a list of PDB chain IDs or AlphaFold UniProt IDs below. The PDB chain IDs are the same as the record names such as "1HHO_A". The UniProt ID is the text between "AF-" and "-F1". For example, the UniProt ID for the record name "AF-P69905-F1-model_v4" is "P69905". Chain ID List: BCIF/MMTF ID: PDB ID: Very high (pLDDT > 90) Confident (90 > pLDDT > 70) Low (70 > pLDDT > 50) Very low (pLDDT < 50) AlphaFold Uniprot ID: PAE Map: NCBI Protein Accession: PDB File: Multiple PDB Files: The custom JSON file on residue colors has the following format for proteins("ALA" and "ARG") and nucleotides("G" and "A"): {"ALA":"#C8C8C8", "ARG":"#145AFF", ..., "G":"#008000", "A":"#6080FF", ...} Residue Color File: The custom file for the structure has two columns separated by space or tab: residue number, and score in the range of 0-100. If you click "Apply Custom Color" button, the scores 0, 50 and 100 correspond to the three colors specified below. If you click "Apply Custom Tube", the selected residues will be displayed in a style similar to "B-factor Tube". Custom File: 1. Score to Color: 0: 50: 100: or 2. You can define your own reference numbers in a custom file using Excel, and then export it as a CSV file. An example file is shown below with cells separated by commas. refnum,11,12,,21,22,,10C,11C,20CThe first row defines the reference residue numbers, which could be any strings. The 1st cell could be anything. The rest cells are reference residue numbers (e.g., 11, 21, 10C, etc.) or empty cells. Each chain has a separate row. The first cell of the second row is the chain ID "1TUP_A". The rest cells are the corresponding real residue numbers for reference residue numbers in the first row. For example, the reference numbers for residues 100, 101, and 132 in the chain 1TUP_A are 11, 12, and 22, respectively. The fourth row shows another set of reference numners for the chain "1TUP_C". It could be a chain from a different structure. To select all residues corresponding to the reference numbers, you can simplay replace ":" with "%" in the Specification. For example, "%12" selects the residue 101 in 1TUP_A and the residue 111 in 1TUP_B. ".A%12" has the chain "A" filter and selects the residue 101 in 1TUP_A. Custom File: ID1: ID2: VAST+ based on VAST: VAST+ based on TM-align: All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: (Note: To align chains in custom PDB files, you could load them in "File > Open File > PDB Files (appendable)" and click "Analysis > Defined Sets". Finally select multiple chains in Defined Sets and click "File > Realign Selection".) All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: The sequence alignment (followed by structure alignment) is based on residue numbers in the First/Master chain: (Note: To align chains in custom PDB files, you could load them in "File > Open File > PDB Files (appendable)" and click "Analysis > Defined Sets". Finally select multiple chains in Defined Sets and click "File > Realign Selection".) All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: Each alignment is defined as " | "-separated residue lists in one line. "10-50" means a range of residues from 10 to 50. Option 1: Option 2: All chains will be aligned to the first chain in the comma-separated chain IDs. Each chain ID has the form of PDBID_chain (e.g., 1HHO_A, case sensitive) or UniprotID (e.g., P69905 for AlphaFold structures). Chain IDs: Each alignment is defined as " | "-separated residue lists in one line. "10-50" means a range of residues from 10 to 50. Please specify the mutations with a comma separated mutation list. Each mutation can be specified as "[uppercase PDB ID or AlphaFold UniProt ID]_[Chain Name]_[Residue Number]_[One Letter Mutant Residue]". E.g., the mutation of N501Y in the E chain of PDB 6M0J can be specified as "6M0J_E_501_Y". For AlphaFold structures, the "Chain ID" is "A". If you load a custom structure without PDB or UniProt ID, you can open "Seq. & Annotations" window and find the chain ID such as "stru_A". The part before the underscore is the structure ID, which can be used to specify the mutation such as "stru_A_...". Remember to choose "Show Mutation in: Current Page". Mutations: ID Type: PDB IDAlphaFold UniProt ID Show Mutation in: Current PageNew Page Mol2 File: SDF File: XYZ File: URL in the same host: Multiple mmCIF Files: mmCIF ID: Note: The "biological unit" is the biochemically active form of a biomolecule, or Note: The "biological unit" is the biochemically active form of a biomolecule, BLAST search with the protein sequence ID or FASTA sequence as input. If the protein accession is not a PDB chain, the corresponding AlphaFold UniProt structure is used. Enter a protein sequence ID (or FASTA sequence) and the aligned protein accession, which can be found using the Protein Sequence ID(NCBI protein accession of a sequence): or FASTA sequence: Aligned Protein Accession (or a chain of a PDB): ESM Metagenomic Atlas. The sequence should be less than 400 characters. For any sequence longer than 400, please see the discussion here. The sequence to structure prediction is done via FASTA sequence: Protein/Gene name: PubChem CID/Name/InchI: Chemical SMILES: Share Link URL: Collection File: Structures: 2fofc contour at default threshold or at: σ fofc contour at default threshold or at: σ 2fofc contour at default threshold or at: σ URL in the same host: fofc contour at default threshold or at: σ URL in the same host: Custom Color: Grid Size: Salt Concentration: M Potential contour at: kT/e(25.6mV at 298K) Note: Only the selected residues are used for DelPhi potential calculation by solving linear Poisson-Boltzmann equation. Grid Size: Salt Concentration: M Surface with max potential at: kT/e(25.6mV at 298K) Surface: Opacity: Wireframe: Note: Only the selected residues are used for DelPhi potential calculation by solving linear Poisson-Boltzmann equation. Potential contour at: kT/e(25.6mV at 298K) Note: Always load a PDB file before loading a PQR or DelPhi potential file. Potential contour at: kT/e(25.6mV at 298K) Grid Size: Salt Concentration: M PQR URL in the same host: Phi URL in the same host: Cube URL in the same host: Note: Always load a PDB file before loading a PQR or DelPhi potential file. Symmetry: Distance: Contact Type:
4. Sort Interactions on: to show two lines of residue nodes to show map with atom details to show interactions with strength parameters in 0-200:
(Note: you can also adjust thresholds at #1 to add/remove interactions.) 5. and select new sets 1. Select sets below or use your current selection: 2. 1. Select sets below or use your current selection. 2. 1. Select sets below or use your current selection: 2. Overall maximum RMSD: Å 3. 1. Select sets below: 2. 1. Select sets below: 2. 1. Select sets below: 2. 1. Select sets below: 2. Hold Ctrl key to select multiple nodes/lines. Green: H-Bonds; Cyan: Salt Bridge/Ionic; Grey: Contacts Magenta: Halogen Bonds; Red: π-Cation; Blue: π-Stacking Scale: Hold Ctrl key to select multiple nodes. Scale: Note: Nodes/Residues can be dragged. Both nodes and dashed lines/interactions can be clicked to select residues. Color legend for interactions (dashed lines): Green: H-Bonds; Cyan: Salt Bridge/Ionic; Grey: Contacts Magenta: Halogen Bonds; Red: π-Cation; Blue: π-Stacking Scale: Hold Ctrl key to select multiple nodes. Scale: Hold Ctrl key to select multiple nodes. Scale:
Contour at: σ Contour at: σ Contour at: % of maximum EM values 1. Select the first set: 2. Sphere with a radius: Å 3. Select the second set to apply the sphere: 4. the sphere around the first set of atoms interacting/contacting residue pairs in a file 1. Extracellular membrane Z-axis position: Å 2. intracellular membrane Z-axis position: Å 3. the adjusted membranes 1. Z-axis position of the first X-Y plane: Å 2. Z-axis position of the second X-Y plane: Å 3. the region between the planes to Defined Sets 2. Size: 3. Color: 4. Pick TWO atoms while holding "Alt" key 5. 2. Size: 3. Color: 4. 1. Pick TWO atoms while holding "Alt" key 2. Line Color: 3. 1. Pick TWO atoms while holding "Alt" key 2. Color: 3. 1. Select two sets
3. 1. Select two sets
2. Line style: 3. Line radius: 4. Color: 5. Opacity: 6. 1. Select a set: 2. Shape: 3. Radius: 4. Color: 5. Opacity: 6. 1. Select sets for pairwise distances
Note: Each set is represented by a vector, which is the X-axis of the principle axes. The angles between the vectors are then calculated. 1. Select sets for pairwise angles
1. Pick TWO atoms while holding "Alt" key 2. Coil Radius: (for coils, default 0.3) Stick Radius: (for sticks, default 0.4) Cross-Linkage Radius: (for cross-linkages, default 0.4) Trace Radius: (for C alpha trace, O3' trace, default 0.4) Ribbon Thickness: (for helix and sheet ribbons, nucleotide ribbons, default 0.2) Protein Ribbon Width: (for helix and sheet ribbons, default 1.3) Nucleotide Ribbon Width: (for nucleotide ribbons, default 0.8) Ball Scale: (for styles 'Ball and Stick' and 'Dot', default 0.3) 1. Shininess: (for the shininess of the 3D objects, default 40) 2. Three directional lights: Key Light: (for the light strength of the key light, default 0.8) Fill Light: (for the light strength of the fill light, default 0.4) Back Light: (for the light strength of the back light, default 0.2) 3. Thickness: Line Radius: (for stabilizers, hydrogen bonds, distance lines, default 0.1) Coil Radius: (for coils, default 0.3) Stick Radius: (for sticks, default 0.4) Cross-Linkage Radius: (for cross-linkages, default 0.4) Trace Radius: (for C alpha trace, O3' trace, default 0.4) Ribbon Thickness: (for helix and sheet ribbons, nucleotide ribbons, default 0.2) Protein Ribbon Width: (for helix and sheet ribbons, default 1.3) Nucleotide Ribbon Width: (for nucleotide ribbons, default 0.8) Ball Scale: (for styles 'Ball and Stick' and 'Dot', default 0.3) 4. Show Glycan Cartoon: (0: hide, 1: show, default 0) 5. Show Membrane: (0: hide, 1: show, default 1) 6. Enlarge Command Window: (0: Regular, 1: Large, default 0) 1. URLs Used in Browsers Please copy one of the URLs below. They show the same result. (To add a title to share link, click "Windows > Your Note" and click "File > Share Link" again.) Original URL with commands: Lifelong Short URL:(To replace this URL, send a pull request to update share.html at iCn3D GitHub) Lifelong Short URL + Window Title:(To update the window title, click "Analysis > Your Note/Window Title".) 2. Commands Used in Jupyter Noteboook Please copy the following commands into a cell in Jupyter Notebook to show the same result. More details are at https://github.com/ncbi/icn3d/tree/master/jupyternotebook. Annotations:
Zoom: mouse wheel; Move: left button; Select Multiple Nodes: Ctrl Key and drag an Area Force on Nodes: Label Size: Internal Edges: Color each residue based on the percentage of solvent accessilbe surface area. The color ranges from blue, to white, to red for a percentage of 0, 35(variable), and 100, respectively. Middle Percentage(White): % Select residue based on the percentage of solvent accessilbe surface area. The values are in the range of 0-100. Min Percentage: % Max Percentage: % Select residue based on B-factor/pLDDT. The values are in the range of 0-100. Min B-factor/pLDDT: % Max B-factor/pLDDT: % X: Y: Z: Vector 2, X: Y: Z: The angle is: degree. 1: 5: 9: 13: 2: 6: 10: 14: 3: 7: 11: 15: Choose an Ig template for selected residues: Choose an Ig template to align with selected residues: |
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Ligand Name: Cysteine Sulfenic Acid | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) in complex with K00007 | PDB:6YG4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGQVWKM153 RFRKTGHVIA163 VKQMRRSGNK173 EENKRILMDL 183 DVVLKSHDCP193 YIVQCFGTFI203 TNTDVFIAME213 LMGTAEKLKK224 RMQGPIPERI 234 LGKMTVAIVK244 ALYYLKEKHG254 VIHRDVKPSN264 ILLDERGQIK274 LDFGISGIRA 319 DVWSLGISLV329 ELATGQFPYK339 NCKTDFEVLT349 KVLQEEPPLL359 PGHMGFSGDF 369 QSFVKDCLTK379 DHRKRPKYNK389 LLEHSFIKRY399 ETLEVDVASW409 FKDVMAKT |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CSO or .CSO2 or .CSO3 or :3CSO;style chemicals stick;color identity;select .A:196 or .A:257 or .A:263 or .A:264 or .A:265 or .A:266 or .A:274 or .A:275 or .A:277 or .A:278 or .A:280; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Click to View More Binding Site Information of This Target and Ligand Pair | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Ligand Name: N-[3-(6-methyl-1H-indazol-3-yl)phenyl]prop-2-enamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | MAP2K7 C276S mutant-inhibitor | PDB:5Z1D | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.28 Å | Mutation | No | [2] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGQVWKM153 RFRKTGHVIA163 VKQMRRSGNK173 EENKRILMDL 183 DVVLKSHDCP193 YIVQCFGTFI203 TNTDVFIAME213 LMGTCAEKLK223 KRMQGPIPER 233 ILGKMTVAIV243 KALYYLKEKH253 GVIHRDVKPS263 NILLDERGQI273 KLSDFGISGC 296 AAYMAPERID306 PPRADVWSLG325 ISLVELATGQ335 FPYKNCKTDF345 EVLTKVLQEE 355 PPLLPGHMGF365 SGDFQSFVKD375 CLTKDHRKRP385 KYNKLLEHSF395 IKRYETLEVD 405 VASWFKDVMA415 KTES
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .95U or .95U2 or .95U3 or :395U;style chemicals stick;color identity;select .A:142 or .A:150 or .A:163 or .A:165 or .A:182 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Click to View More Binding Site Information of This Target and Ligand Pair | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Ligand Name: 5Z-7-Oxozeaenol | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | THE STRUCTURE OF MAP2K7 IN COMPLEX WITH 5Z-7-oxozeaenol | PDB:3WZU | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 3.01 Å | Mutation | No | [3] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
GYLTIGGQRY
129 QAEINDLENL139 GEMGSGTCGQ149 VWKMRFRKTG159 HVIAVKQMRR169 SGNKVVLKSH 190 DCPYIVQCFG200 TFITNTDVFI210 AMELMGTCAE220 KLKKRMQGPI230 PERILGKMTV 240 AIVKALYYLK250 EKHGVIHRDV260 KPSNILLDER270 GQIKLCDFGA294 GCAAYMAPER 304 IDPPPDYDIR318 ADVWSLGISL328 VELATGQFPY338 KNCKTDFEVL348 TKVLQEEPPL 358 LPGHMGFSGD368 FQSFVKDCLT378 KDHRKRPKYN388 KLLEHSFIKR398 YETLEVDVAS 408 WFKDVMAKTE418
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1FM or .1FM2 or .1FM3 or :31FM;style chemicals stick;color identity;select .A:142 or .A:143 or .A:145 or .A:146 or .A:147 or .A:150 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:221 or .A:263 or .A:264 or .A:266 or .A:276; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.532
GLY143
3.534
GLY145
3.409
THR146
2.511
CYS147
3.953
VAL150
4.044
ALA163
3.750
LYS165
3.113
VAL196
4.482
MET212
2.965
GLU213
2.878
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Ligand Name: 3-(1H-indazol-3-yl)-5-(prop-2-enoylamino)-N-prop-2-ynyl-benzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MAP2K7 complexed with a covalent inhibitor 12 | PDB:7CBX | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.06 Å | Mutation | Yes | [4] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGSGTCG148 QVWKMRFRKT158 GHVIAVKQMR168 RSGNKEENKR 178 ILMDLDVVLK188 SHDCPYIVQC198 FGTFITNTDV208 FIAMELMGTS218 AEKLKKRMQG 228 PIPERILGKM238 TVAIVKALYY248 LKEKHGVIHR258 DVKPSNILLD268 ERGQIKLCDF 278 GISGRCAAYM300 APERIDPPDI317 RADVWSLGIS327 LVELATGQFP337 YKNCKTDFEV 347 LTKVLQEEPP357 LLPGHMGFSG367 DFQSFVKDCL377 TKDHRKRPKY387 NKLLEHSFIK 397 RYETLEVDVA407 SWFKDVMAKT417 E
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FU6 or .FU62 or .FU63 or :3FU6;style chemicals stick;color identity;select .A:142 or .A:144 or .A:152 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: 1-[(3R)-3-[4-amino-3-[1-(2-phenylethyl)triazol-4-yl]pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with phenethyltriazole-substituted pyrazolopyrimidine | PDB:7OVI | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.95 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGGQ149 VWKMRFRKTG159 HVIAVKQMRR169 SGNKEENKRI 179 LMDLDVVLKS189 HDCPYIVQCF199 GTFITNTDVF209 IAMELMGTCA219 EKLKKRMQGP 229 IPERILGKMT239 VAIVKALYYL249 KEKHGVIHRD259 VKPSNILLDE269 RGQIKLCDFG 279 IRADVWSLGI326 SLVELATGQF336 PYKNCKTDFE346 VLTKVLQEEP356 PLLPGHMGFS 366 GDFQSFVKDC376 LTKDHRKRPK386 YNKLLEHSFI396 KRYETLEVDV406 ASWFKDVMAK 416 TE
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2GI or .2GI2 or .2GI3 or :32GI;style chemicals stick;color identity;select .A:142 or .A:143 or .A:145 or .A:150 or .A:163 or .A:165 or .A:179 or .A:182 or .A:183 or .A:186 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.615
GLY143
3.476
GLY145
4.515
VAL150
4.265
ALA163
3.780
LYS165
3.441
ILE179
3.475
ASP182
3.710
LEU183
3.535
VAL186
4.284
VAL196
3.760
ILE210
3.960
MET212
3.457
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Ligand Name: 1-[(3R)-3-[4-amino-3-[1-(5-bromo-2-hydroxyphenyl)triazol-4-yl]pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with 5-bromo-2-hydroxyphenyl-substituted pyrazolopyrimidine | PDB:7OVK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.05 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGGQVW151 KMRFRKTGHV161 IAVKQMRRSG171 NKEENKRILM 181 DLDVVLKSHD191 CPYIVQCFGT201 FITNTDVFIA211 MELMGTCAEK221 LKKRMQGPIP 231 ERILGKMTVA241 IVKALYYLKE251 KHGVIHRDVK261 PSNILLDERG271 QIKLCDFADV 321 WSLGISLVEL331 ATGQFPYKNC341 KTDFEVLTKV351 LQEEPPLLPG361 HMGFSGDFQS 371 FVKDCLTKDH381 RKRPKYNKLL391 EHSFIKRYET401 LEVDVASWFK411 DVMAKT |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2I5 or .2I52 or .2I53 or :32I5;style chemicals stick;color identity;select .A:142 or .A:143 or .A:150 or .A:163 or .A:165 or .A:179 or .A:182 or .A:183 or .A:186 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:262 or .A:263 or .A:266 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.416
GLY143
3.462
VAL150
4.233
ALA163
3.789
LYS165
3.982
ILE179
4.263
ASP182
3.622
LEU183
3.598
VAL186
4.459
VAL196
3.954
ILE210
4.051
MET212
3.481
GLU213
2.853
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Ligand Name: 1-[(3R)-3-(4-amino-3-naphthalen-1-ylpyrazolo[3,4-d]pyrimidin-1-yl)piperidin-1-yl]prop-2-en-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Structure of the mitogen activated kinase kinase 7 in complex with pyrazolopyrimidine 1k | PDB:6QG7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGTC147 GQVWKMRFRK157 TGHVIAVKQM167 RRSGNKEENK 177 RILMDLDVVL187 KSHDCPYIVQ197 CFGTFITNTD207 VFIAMELMGT217 CAEKLKKRMQ 227 GPIPERILGK237 MTVAIVKALY247 YLKEKHGVIH257 RDVKPSNILL267 DERGQIKLCD 277 FGISGRLAGC296 AAYMAPERID306 PIRADVWSLG325 ISLVELATGQ335 FPYKNCKTDF 345 EVLTKVLQEE355 PPLLPGHMGF365 SGDFQSFVKD375 CLTKDHRKRP385 KYNKLLEHSF 395 IKRYETLEVD405 VASWFKDVMA415 KT
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6HL or .6HL2 or .6HL3 or :36HL;style chemicals stick;color identity;select .A:142 or .A:143 or .A:145 or .A:146 or .A:150 or .A:163 or .A:165 or .A:182 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.816
GLY143
3.598
GLY145
4.257
THR146
4.953
VAL150
4.019
ALA163
3.124
LYS165
3.627
ASP182
3.230
VAL196
4.819
ILE210
4.971
MET212
3.330
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Ligand Name: 1-[(3R)-3-[3-[1-(4-acetylphenyl)triazol-4-yl]-4-aminopyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | The structure of MKK7 in complex with the covalent 4-amino-pyrazolopyrimidine 4a | PDB:6IB2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [7] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGQVWK152 MRFRKTGHVI162 AVKQMRRSGN172 KEENKRILMD 182 LDVVLKSHDC192 PYIVQCFGTF202 ITNTDVFIAM212 ELMGTCAEKL222 KKRMQGPIPE 232 RILGKMTVAI242 VKALYYLKEK252 HGVIHRDVKP262 SNILLDERGQ272 IKLCDFAYMA 301 PERIDRADVW322 SLGISLVELA332 TGQFPYKKCK342 TDFEVLTKVL352 QEEPPLLPGH 362 MGFSGDFQSF372 VKDCLTKDHR382 KRPKYNKLLE392 HSFIKRYETL402 EVDVASWFKD 412 VMAKT
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .862 or .8622 or .8623 or :3862;style chemicals stick;color identity;select .A:142 or .A:143 or .A:150 or .A:163 or .A:165 or .A:178 or .A:179 or .A:182 or .A:183 or .A:186 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:218 or .A:220 or .A:221 or .A:262 or .A:263 or .A:266 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.192
GLY143
3.611
VAL150
4.298
ALA163
3.761
LYS165
3.552
ARG178
4.140
ILE179
3.061
ASP182
3.268
LEU183
3.326
VAL186
4.585
VAL196
3.647
ILE210
4.930
MET212
3.250
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Ligand Name: 1-[(3R)-3-[4-amino-3-(4-hydroxyphenyl)pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Structure of the mitogen activated kinase kinase 7 in complex with pyrazolopyrimidine inhibitor 1h | PDB:6QG4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGQR
128 YQAEINDLEN138 LGEMGQVWKM153 RFRKTGHVIA163 VKQMRRSGNK173 EENKRILMDL 183 DVVLKSHDCP193 YIVQCFGTFI203 TNTDVFIAME213 LMGTCAEKLK223 KRMQGPIPER 233 ILGKMTVAIV243 KALYYLKEKH253 GVIHRDVKPS263 NILLDERGQI273 KLCDFGISGR 283 AAYMAPERID306 PIRADVWSLG325 ISLVELATGQ335 FPYKNCKTDF345 EVLTKVLQEE 355 PPLLPGHMGF365 SGDFQSFVKD375 CLTKDHRKRP385 KYNKLLEHSF395 IKRYETLEVD 405 VASWFKDVMA415 KT
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J0E or .J0E2 or .J0E3 or :3J0E;style chemicals stick;color identity;select .A:142 or .A:143 or .A:150 or .A:163 or .A:165 or .A:182 or .A:186 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:221 or .A:263 or .A:266 or .A:276; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: 1-[(3R)-3-[4-amino-3-[1-(2,2-difluoro-2-phenylethyl)triazol-4-yl]pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with difluoro-phenethyltriazole-substituted pyrazolopyrimidine | PDB:7OVJ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.35 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGGQ149 VWKMRFRKTG159 HVIAVKQMRR169 SGNKEENKRI 179 LMDLDVVLKS189 HDCPYIVQCF199 GTFITNTDVF209 IAMELMGTCA219 EKLKKRMQGP 229 IPERILGKMT239 VAIVKALYYL249 KEKHGVIHRD259 VKPSNILLDE269 RGQIKLCDFG 279 GCAAYMAPER304 IDPIRADVWS323 LGISLVELAT333 GQFPYKNCKT343 DFEVLTKVLQ 353 EEPPLLPGHM363 GFSGDFQSFV373 KDCLTKDHRK383 RPKYNKLLEH393 SFIKRYETLE 403 VDVASWFKDV413 MAKTRS
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .24N or .24N2 or .24N3 or :324N;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:150 or .A:163 or .A:165 or .A:179 or .A:182 or .A:183 or .A:186 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.162
GLY143
3.736
SER144
4.859
VAL150
4.009
ALA163
3.911
LYS165
3.709
ILE179
3.261
ASP182
3.570
LEU183
3.455
VAL186
4.450
VAL196
3.827
ILE210
3.994
MET212
3.254
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Ligand Name: 1-[(3R)-3-[4-amino-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Structure of the mitogen activated kinase kinase 7 in complex with pyrazolopyrimidine 1m | PDB:6QHR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.52 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
KQTGYLTIGG
126 QRYQAEINDL136 ENLGEMGSGT146 CGQVWKMRFR156 KTGHVIAVKQ166 MRRSGNKEEN 176 KRILMDLDVV186 LKSHDCPYIV196 QCFGTFITNT206 DVFIAMELMG216 TCAEKLKKRM 226 QGPIPERILG236 KMTVAIVKAL246 YYLKEKHGVI256 HRDVKPSNIL266 LDERGQIKLC 276 DFGISGRLAG295 CAAYMAPERI305 DPPYDIRADV321 WSLGISLVEL331 ATGQFPYKNC 341 KTDFEVLTKV351 LQEEPPLLPG361 HMGFSGDFQS371 FVKDCLTKDH381 RKRPKYNKLL 391 EHSFIKRYET401 LEVDVASWFK411 DVMAKT
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J3N or .J3N2 or .J3N3 or :3J3N;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:146 or .A:150 or .A:163 or .A:164 or .A:165 or .A:182 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.936
GLY143
4.514
SER144
3.574
THR146
4.813
VAL150
4.078
ALA163
3.623
VAL164
4.903
LYS165
3.360
ASP182
3.310
ILE210
3.619
MET212
3.076
|
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Ligand Name: 1-[(3R)-3-(4-amino-3-ethynylpyrazolo[3,4-d]pyrimidin-1-yl)piperidin-1-yl]prop-2-en-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | The structure of MKK7 in complex with the covalent 4-amino-pyrazolopyrimidine 3a | PDB:6IB0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [7] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
KQTGYLTIGG
126 QRYQAEINDL136 ENLGEMGSGT146 CGQVWKMRFR156 KTGHVIAVKQ166 MRRSGNKEEN 176 KRILMDLDVV186 LKSHDCPYIV196 QCFGTFITNT206 DVFIAMELMG216 TCAEKLKKRM 226 QGPIPERILG236 KMTVAIVKAL246 YYLKEKHGVI256 HRDVKPSNIL266 LDERGQIKLC 276 DFGISGRAGC296 AAYMAPERID306 PPDPTKPDYD316 IRADVWSLGI326 SLVELATGQF 336 PYKNCKTDFE346 VLTKVLQEEP356 PLLPGHMGFS366 GDFQSFVKDC376 LTKDHRKRPK 386 YNKLLEHSFI396 KRYETLEVDV406 ASWFKDVMAK416
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .H8Z or .H8Z2 or .H8Z3 or :3H8Z;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:145 or .A:146 or .A:150 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:221 or .A:263 or .A:266 or .A:276; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.324
GLY143
4.091
SER144
4.263
GLY145
3.765
THR146
4.915
VAL150
3.722
ALA163
4.008
LYS165
4.807
VAL196
3.549
MET212
3.784
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Ligand Name: 1-[(3R)-3-(4-amino-3-iodopyrazolo[3,4-d]pyrimidin-1-yl)piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Structure of the mitogen activated kinase kinase 7 in complex with pyrazolopyrimidin 1b | PDB:6QFT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGQR
128 YQAEINDLEN138 LGEMGSGTCG148 QVWKMRFRKT158 GHVIAVKQMR168 RSGNKEENKR 178 ILMDLDVVLK188 SHDCPYIVQC198 FGTFITNTDV208 FIAMELMGTC218 AEKLKKRMQG 228 PIPERILGKM238 TVAIVKALYY248 LKEKHGVIHR258 DVKPSNILLD268 ERGQIKLCDF 278 GISGRCAAYM300 APERIDPRAD320 VWSLGISLVE330 LATGQFPYKN340 CKTDFEVLTK 350 VLQEEPPLLP360 GHMGFSGDFQ370 SFVKDCLTKD380 HRKRPKYNKL390 LEHSFIKRYE 400 TLEVDVASWF410 KDVMAK
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J0B or .J0B2 or .J0B3 or :3J0B;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:145 or .A:146 or .A:150 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:263 or .A:266 or .A:276; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.488
GLY143
3.781
SER144
3.914
GLY145
4.820
THR146
3.324
VAL150
3.685
ALA163
3.871
LYS165
4.330
VAL196
4.591
MET212
3.726
|
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Ligand Name: 1-[(3R)-3-(4-aminopyrazolo[3,4-d]pyrimidin-1-yl)piperidin-1-yl]propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Dual specificity mitogen-activated protein kinase kinase 7 in complex with pyrazolopyrimidine 1a | PDB:6QHO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGTC147 GQVWKMRFRK157 TGHVIAVKQM167 RRSGNKEENK 177 RILMDLDVVL187 KSHDCPYIVQ197 CFGTFITNTD207 VFIAMELMGT217 CAEKLKKRMQ 227 GPIPERILGK237 MTVAIVKALY247 YLKEKHGVIH257 RDVKPSNILL267 DERGQIKLCD 277 FGISGRYMAP302 ERIDPRADVW322 SLGISLVELA332 TGQFPYKNCK342 TDFEVLTKVL 352 QEEPPLLPGH362 MGFSGDFQSF372 VKDCLTKDHR382 KRPKYNKLLE392 HSFIKRYETL 402 EVDVASWFKD412 VMAKT
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .J3H or .J3H2 or .J3H3 or :3J3H;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:146 or .A:150 or .A:163 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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Ligand Name: 3-(1H-indazol-3-yl)-N-[[1-(2-methylphenyl)triazol-4-yl]methyl]-5-(propanoylamino)benzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with tolyl-substituted indazole | PDB:7OVN | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGTQ149 VWKMRFRKTG159 HVIAVKQMRR169 SGNKEENKRI 179 LMDLDVVLKS189 HDCPYIVQCF199 GTFITNTDVF209 IAMELMGTCA219 EKLKKRMQGP 229 IPERILGKMT239 VAIVKALYYL249 KEKHGVIHRD259 VKPSNILLDE269 RGQIKLCDFG 279 ISGRAGCAAY299 MAPERIDPPD309 DIRADVWSLG325 ISLVELATGQ335 FPYKNCKTDF 345 EVLTKVLQEE355 PPLLPGHMGF365 SGDFQSFVKD375 CLTKDHRKRP385 KYNKLLEHSF 395 IKRYETLEVD405 VASWFKDVMA415 KTE
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .2I8 or .2I82 or .2I83 or :32I8;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:152 or .A:163 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:269 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.892
GLY143
4.468
SER144
3.549
LYS152
3.138
ALA163
3.732
VAL196
4.195
MET212
3.901
GLU213
2.596
LEU214
3.474
MET215
3.051
|
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Ligand Name: 3-(1H-indazol-3-yl)-N-[[1-[(1R,2R)-2-methoxycyclohexyl]triazol-4-yl]methyl]-5-(propanoylamino)benzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with methoxycyclohexyl-substituted indazole | PDB:7OVL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGQVWK152 MRFRKTGHVI162 AVKQMRRSGN172 KEENKRILMD 182 LDVVLKSHDC192 PYIVQCFGTF202 ITNTDVFIAM212 ELMGTCAEKL222 KKRMQGPIPE 232 RILGKMTVAI242 VKALYYLKEK252 HGVIHRDVKP262 SNILLDERGQ272 IKLCDFGISA 294 GCAAYMAPER304 IDPPDYDIRA319 DVWSLGISLV329 ELATGQFPYK339 NCKTDFEVLT 349 KVLQEEPPLL359 PGHMGFSGDF369 QSFVKDCLTK379 DHRKRPKYNK389 LLEHSFIKRY 399 ETLEVDVASW409 FKDVMAKTE
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1XZ or .1XZ2 or .1XZ3 or :31XZ;style chemicals stick;color identity;select .A:142 or .A:143 or .A:150 or .A:152 or .A:161 or .A:163 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:269 or .A:276; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.646
GLY143
3.626
VAL150
4.895
LYS152
3.130
VAL161
3.839
ALA163
4.162
VAL196
4.448
MET212
4.058
GLU213
2.899
LEU214
3.234
|
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Ligand Name: N-[(1-cyclobutyltriazol-4-yl)methyl]-3-(1H-indazol-3-yl)-5-(propanoylamino)benzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Protein kinase MKK7 in complex with cyclobutyl-substituted indazole | PDB:7OVM | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGTQ149 VWKMRFRKTG159 HVIAVKQMRR169 SGNKEENKRI 179 LMDLDVVLKS189 HDCPYIVQCF199 GTFITNTDVF209 IAMELMGTCA219 EKLKKRMQGP 229 IPERILGKMT239 VAIVKALYYL249 KEKHGVIHRD259 VKPSNILLDE269 RGQIKLCDFG 279 ISGRGCAAYM300 APERIDPPDD316 IRADVWSLGI326 SLVELATGQF336 PYKNCKTDFE 346 VLTKVLQEEP356 PLLPGHMGFS366 GDFQSFVKDC376 LTKDHRKRPK386 YNKLLEHSFI 396 KRYETLEVDV406 ASWFKDVMAK416 TE
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .21I or .21I2 or .21I3 or :321I;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:150 or .A:152 or .A:161 or .A:163 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:263 or .A:266 or .A:269 or .A:276 or .A:277; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.234
GLY143
3.114
SER144
3.793
VAL150
4.749
LYS152
3.566
VAL161
4.409
ALA163
4.153
VAL196
3.590
MET212
3.878
GLU213
2.725
LEU214
3.358
|
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Ligand Name: (R)-1-(3-(4-amino-3-(4-phenoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl)piperidin-1-yl)propan-1-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) in complex with ibrutnib, with covalent and allosteric binding modes | PDB:6YG2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGTC147 GQVWKMRFRK157 TGHVIAVKQM167 RRSGNKEENK 177 RILMDLDVVL187 KSHDCPYIVQ197 CFGTFITNTD207 VFIAMELMGT217 CAEKLKKRMQ 227 GPIPERILGK237 MTVAIVKALY247 YLKEKHGVIH257 RDVKPSNILL267 DERGQIKLCD 277 FGISGCAAYM300 APERIDPPDP310 TKPDYDIRAD320 VWSLGISLVE330 LATGQFPYKN 340 CKTDFEVLTK350 VLQEEPPLLP360 GHMGFSGDFQ370 SFVKDCLTKD380 HRKRPKYNKL 390 LEHSFIKRYE400 TLEVDVASWF410 KDVMAKTESP420
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .8E8 or .8E82 or .8E83 or :38E8;style chemicals stick;color identity;select .A:142 or .A:143 or .A:144 or .A:145 or .A:146 or .A:150 or .A:163 or .A:165 or .A:179 or .A:182 or .A:183 or .A:186 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276 or .A:278; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
MET142
3.239
GLY143
3.808
SER144
3.584
GLY145
3.220
THR146
4.879
VAL150
4.099
ALA163
4.002
LYS165
3.303
ILE179
3.233
ASP182
3.582
LEU183
3.538
VAL186
4.815
VAL196
3.959
|
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Ligand Name: N-(4-((2-((4-(4-Methylpiperazin-1-Yl)phenyl)amino)-7h-Pyrrolo[2,3-D]pyrimidin-4-Yl)oxy)phenyl)acrylamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) covalently bound with CPT1-70-1 | PDB:6YG3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.05 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGSGTCG148 QVWKMRFRKT158 GHVIAVKQMR168 RSGNKEENKR 178 ILMDLDVVLK188 SHDCPYIVQC198 FGTFITNTDV208 FIAMELMGTC218 AEKLKKRMQG 228 PIPERILGKM238 TVAIVKALYY248 LKEKHGVIHR258 DVKPSNILLD268 ERGQIKLCDF 278 GISGRLRADV321 WSLGISLVEL331 ATGQFPYKNC341 KTDFEVLTKV351 LQEEPPLLPG 361 HMGFSGDFQS371 FVKDCLTKDH381 RKRPKYNKLL391 EHSFIKRYET401 LEVDVASWFK 411 DVMAK
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6HF or .6HF2 or .6HF3 or :36HF;style chemicals stick;color identity;select .A:141 or .A:142 or .A:143 or .A:150 or .A:163 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:263 or .A:266 or .A:276; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: N-[4-[(4-ethylpiperazin-1-yl)methyl]-3-(trifluoromethyl)phenyl]-4-methyl-3-[2-[[(3S)-1-propanoylpyrrolidin-3-yl]amino]pyrimidin-4-yl]oxybenzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) covalently bound with type-II inhibitor TL10-105 | PDB:6YG6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.15 Å | Mutation | Yes | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGSGQVW151 KMRFRKTGHV161 IAVKQMRRSG171 NKEENKRILM 181 DLDVVLKSHD191 CPYIVQCFGT201 FITNTDVFIA211 MELMGTCAEK221 LKKRMQGPIP 231 ERILGKMTVA241 IVKALYYLKE251 KHGVIHRDVK261 PSNILLDERG271 QIKLCDFGAG 295 CAAYMAPERI305 DPPDPTKPDY315 DIRADVWSLG325 ISLVELATGQ335 FPYKNCKTDF 345 EVLTKVLQEE355 PPLLPGHMGF365 SGDFQSFVKD375 CLTKDHRKRP385 KYNKLLEHSF 395 IKRYETLEVD405 VASWFKDVMA415 KTES
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OQ8 or .OQ82 or .OQ83 or :3OQ8;style chemicals stick;color identity;select .A:142 or .A:150 or .A:163 or .A:164 or .A:165 or .A:182 or .A:183 or .A:185 or .A:186 or .A:195 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:249 or .A:255 or .A:256 or .A:257 or .A:258 or .A:263 or .A:266 or .A:275 or .A:276 or .A:277 or .A:278; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
3.945
VAL150
3.818
ALA163
3.810
VAL164
3.779
LYS165
3.478
ASP182
3.751
LEU183
4.173
VAL185
4.962
VAL186
3.111
ILE195
3.641
VAL196
3.464
ILE210
4.011
MET212
3.209
GLU213
3.071
LEU214
3.911
MET215
2.803
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Ligand Name: N-[4-[(4-ethylpiperazin-1-yl)methyl]-3-(trifluoromethyl)phenyl]-4-methyl-3-[2-[[(3R)-1-propanoylpyrrolidin-3-yl]amino]pyrimidin-4-yl]oxybenzamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) covalently bound with type-II inhibitor SB1-G-23 | PDB:6YG7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
QTGYLTIGGQ
127 RYQAEINDLE137 NLGEMGSGQV150 WKMRFRKTGH160 VIAVKQMRRS170 GNKEENKRIL 180 MDLDVVLKSH190 DCPYIVQCFG200 TFITNTDVFI210 AMELMGTCAE220 KLKKRMQGPI 230 PERILGKMTV240 AIVKALYYLK250 EKHGVIHRDV260 KPSNILLDER270 GQIKLCDFGI 280 CAAYMAPERI305 DPPYDIRADV321 WSLGISLVEL331 ATGQFPYKNC341 KTDFEVLTKV 351 LQEEPPLLPG361 HMGFSGDFQS371 FVKDCLTKDH381 RKRPKYNKLL391 EHSFIKRYET 401 LEVDVASWFK411 DVMAKTES
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OQ2 or .OQ22 or .OQ23 or :3OQ2;style chemicals stick;color identity;select .A:142 or .A:143 or .A:150 or .A:163 or .A:164 or .A:165 or .A:182 or .A:185 or .A:186 or .A:195 or .A:196 or .A:210 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:218 or .A:220 or .A:221 or .A:249 or .A:255 or .A:256 or .A:257 or .A:258 or .A:263 or .A:266 or .A:275 or .A:276 or .A:277 or .A:278; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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MET142
4.171
GLY143
4.885
VAL150
3.875
ALA163
4.114
VAL164
4.147
LYS165
3.686
ASP182
3.508
VAL185
4.581
VAL186
4.653
ILE195
3.815
VAL196
3.355
ILE210
4.623
MET212
3.288
GLU213
3.101
LEU214
3.978
MET215
3.107
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Ligand Name: 3-(1H-imidazol-5-ylmethylidene)-5-methoxy-1H-indol-2-one | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) in complex with K00007 | PDB:6YG4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
TGYLTIGGQR
128 YQAEINDLEN138 LGEMGQVWKM153 RFRKTGHVIA163 VKQMRRSGNK173 EENKRILMDL 183 DVVLKSHDCP193 YIVQCFGTFI203 TNTDVFIAME213 LMGTAEKLKK224 RMQGPIPERI 234 LGKMTVAIVK244 ALYYLKEKHG254 VIHRDVKPSN264 ILLDERGQIK274 LDFGISGIRA 319 DVWSLGISLV329 ELATGQFPYK339 NCKTDFEVLT349 KVLQEEPPLL359 PGHMGFSGDF 369 QSFVKDCLTK379 DHRKRPKYNK389 LLEHSFIKRY399 ETLEVDVASW409 FKDVMAKT |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SU9 or .SU92 or .SU93 or :3SU9;style chemicals stick;color identity;select .A:142 or .A:150 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:266 or .A:277; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl}amino)phenyl]acetonitrile | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of MKK7 (MAP2K7) in complex with ASC69 | PDB:6YG5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
KQTGYLTIGG
126 QRYQAEINDL136 ENLGEMGGQV150 WKMRFRKTGH160 VIAVKQMRRS170 GNKEENKRIL 180 MDLDVVLKSH190 DCPYIVQCFG200 TFITNTDVFI210 AMELMGTAEK221 LKKRMQGPIP 231 ERILGKMTVA241 IVKALYYLKE251 KHGVIHRDVK261 PSNILLDERG271 QIKLDFGISG 282 DVWSLGISLV329 ELATGQFPYK339 NCKTDFEVLT349 KVLQEEPPLL359 PGHMGFSGDF 369 QSFVKDCLTK379 DHRKRPKYNK389 LLEHSFIKRY399 ETLEVDVASW409 FKDVMAKTES 419
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .IHH or .IHH2 or .IHH3 or :3IHH;style chemicals stick;color identity;select .A:142 or .A:143 or .A:148 or .A:150 or .A:163 or .A:165 or .A:196 or .A:212 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:221 or .A:266 or .A:277 or .A:278; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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References | Top | ||||
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REF 1 | Catalytic Domain Plasticity of MKK7 Reveals Structural Mechanisms of Allosteric Activation and Diverse Targeting Opportunities. Cell Chem Biol. 2020 Oct 15;27(10):1285-1295.e4. | ||||
REF 2 | Covalent Docking Identifies a Potent and Selective MKK7 Inhibitor. Cell Chem Biol. 2019 Jan 17;26(1):98-108.e5. | ||||
REF 3 | 5Z-7-Oxozeaenol covalently binds to MAP2K7 at Cys218 in an unprecedented manner. Bioorg Med Chem Lett. 2015 Feb 1;25(3):593-6. | ||||
REF 4 | Structural basis for producing selective MAP2K7 inhibitors. Bioorg Med Chem Lett. 2020 Nov 15;30(22):127546. | ||||
REF 5 | Optimization of Covalent MKK7 Inhibitors via Crude Nanomole-Scale Libraries. J Med Chem. 2022 Aug 11;65(15):10341-10356. | ||||
REF 6 | Characterization of Covalent Pyrazolopyrimidine-MKK7 Complexes and a Report on a Unique DFG-in/Leu-in Conformation of Mitogen-Activated Protein Kinase Kinase 7 (MKK7). J Med Chem. 2019 Jun 13;62(11):5541-5546. | ||||
REF 7 | Targeting the MKK7-JNK (Mitogen-Activated Protein Kinase Kinase 7-c-Jun N-Terminal Kinase) Pathway with Covalent Inhibitors. J Med Chem. 2019 Mar 14;62(5):2843-2848. |
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