Binding Site Information of Target
Target General Information | Top | ||||
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Target ID | T01280 | Target Info | |||
Target Name | Beta-site APP-cleaving enzyme 2 (BACE2) | ||||
Synonyms | Theta-secretase; Membrane-associated aspartic protease 1; Memapsin-1; Down region aspartic protease; DRAP; Beta-site amyloid precursor protein cleaving enzyme 2; Beta-site APP cleaving enzyme 2; Beta-secretase 2; Aspartyl protease 1; Aspartic-like protease 56 kDa; Asp 1; ASP21; ASP1; ALP56; AEPLC | ||||
Target Type | Clinical trial Target | ||||
Gene Name | BACE2 | ||||
UniProt ID |
Drug Binding Sites of Target | Top | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Ligand Name: Verubecestat | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 xaperone complex with N-{3-[(5R)-3-amino-2,5-dimethyl-1,1-dioxo-5,6-dihydro-2H-1lambda6,2,4-thiadiazin-5-yl]-4-fluorophenyl}-5-fluoropyridine-2-carboxamide | PDB:7D5B | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.31 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
ANFLAMVDNL
22 QGDSGRGYYL32 EMLIGTPPQK42 LQILVDTGSS52 NFAVAGTPHS62 YIDTYFDTER 72 SSTYRSKGFD82 VTVKYTQGSW92 TGFVGEDLVT102 IPKGFNTSFL112 VNIATIFESE 122 NFFLPGIKWN132 GILGLAYATL142 AKPSSSLETF152 FDSLVTQANI162 PNVFSMQMCG 172 AGLNGGSLVL189 GGIEPSLYKG199 DIWYTPIKEE209 WYYQIEILKL219 EIGGQSLNLD 229 CREYNADKAI239 VDSGTTLLRL249 PQKVFDAVVE259 AVARASLIPE269 FSDGFWTGSQ 279 LACWTNTPWS291 YFPKISIYLR301 DENSSRSFRI311 TILPQLYIQP321 MECYRFGISP 338 STNALVIGAT348 VMEGFYVIFD358 RAQKRVGFAA368 SPCAEIAGAA378 VSEISGPFST 388 EDVASNCVP
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☰7D5B Nodes: OProtein ▢Nucleotide ◇Chemical ▢Biopolymer Lines: Interactions at 4 Å 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: 2ewy | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | Crystal structure of human BACE2 in complex with a hydroxyethylenamine transition-state inhibitor | PDB:2EWY | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 3.10 Å | Mutation | No | [2] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
LAMVDNLQGD
25 SGRGYYLEML35 IGTPPQKLQI45 LVDTGSSNFA55 VAGTPHSYID65 TYFDTERSST 75 YRSKGFDVTV85 KYTQGSWTGF95 VGEDLVTIPK105 GFNTSFLVNI115 ATIFESENFF 125 LPGIKWNGIL135 GLAYATLAKP145 SSSLETFFDS155 LVTQANIPNV165 FSMQMCGANG 184 GSLVLGGIEP194 SLYKGDIWYT204 PIKEEWYYQI214 EILKLEIGGQ224 SLNLDCREYN 234 ADKAIVDSGT244 TLLRLPQKVF254 DAVVEAVARA264 SLIPEFSDGF274 WTGSQLACWT 284 NSETPWSYFP294 KISIYLRDEN304 SSRSFRITIL314 PQLYIQPMMG324 AGLNYECYRF 334 GISPSTNALV344 IGATVMEGFY354 VIFDRAQKRV364 GFAASPCAEI374 AGAAVSEISG 384 PFSTEDVASN394 CVPA
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☰2EWY Nodes: OProtein ▢Nucleotide ◇Chemical ▢Biopolymer Lines: Interactions at 4 Å 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: |
LEU46
3.528
ASP48
2.748
GLY50
3.062
SER51
3.635
VAL85
4.390
LYS86
3.154
TYR87
3.496
THR88
3.126
GLN89
3.622
ASN123
4.840
PHE124
3.466
LEU126
4.172
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Ligand Name: (3S)-3-hydroxy-N-(2-methylpropyl)-N~2~-{[(4S)-17-[(methylsulfonyl)(propyl)amino]-2-oxo-3-azatricyclo[13.3.1.1~6,10~]icosa-1(19),6(20),7,9,15,17-hexaen-4-yl]methyl}-L-norleucinamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 mutant in complex with a macrocyclic compound | PDB:6UJ1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 3.03 Å | Mutation | Yes | [3] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
LAMVDNLQGD
25 SGRGYYLEML35 IGTPPQKLQI45 LVDTGSSNFA55 VAGTPHSYID65 TYFDTERSST 75 YRSKGFDVTV85 KYTQGSWTGF95 VGEDLVTIPK105 GFNTSFLVNI115 ATIFESENFF 125 LPGIKWNGIL135 GLAYATLAKP145 SSSLETFFDS155 LVTQANIPNV165 FSMQMCGAGL 175 PGTNGGSLVL189 GGIEPSLYKG199 DIWYTPIKEE209 WYYQIEILKL219 EIGGQSLNLD 229 CREYNADKAI239 VDSGTTLLRL249 PQKVFDAVVE259 AVARASFSDG273 FWTGSQLACW 283 TNSETPWSYF293 PKISIYLRDE303 NSSRSFRITI313 LPQLYIQPML327 NYECYRFGIS 337 PSTNALVIGA347 TVMEGFYVIF357 DRAQKRVGFA367 ASPCAEIAGA377 AVSEISGPFS 387 TASNCVP
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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 .L3M or .L3M2 or .L3M3 or :3L3M;style chemicals stick;color identity;select .A:27 or .A:28 or .A:46 or .A:48 or .A:50 or .A:51 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:124 or .A:126 or .A:131 or .A:134 or .A:142 or .A:211 or .A:239 or .A:241 or .A:243 or .A:244 or .A:245 or .A:246 or .A:248 or .A:337 or .A:342 or .A:344; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
GLY27
4.131
ARG28
4.248
LEU46
4.225
ASP48
3.352
GLY50
3.108
SER51
4.041
VAL85
3.871
LYS86
3.108
TYR87
3.422
THR88
2.260
GLN89
3.443
PHE124
3.623
LEU126
4.601
TRP131
4.049
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Ligand Name: N-{3-[(2S,5R)-6-amino-2-(fluoromethyl)-5-(methanesulfonyl)-5-methyl-2,3,4,5-tetrahydropyridin-2-yl]-4-fluorophenyl}-6-methoxypyrimidine-4-carboxamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE-2 in complex with ligand 36 | PDB:7N4N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.41 Å | Mutation | No | [4] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
ANFLAMVDNL
22 QGDSGRGYYL32 EMLIGTPPQK42 LQILVDTGSS52 NFAVAGTPHS62 YIDTYFDTER 72 SSTYRSKGFD82 VTVKYTQGSW92 TGFVGEDLVT102 IPKGFNTSFL112 VNIATIFESE 122 NFFLPGIKWN132 GILGLAYATL142 AKPSSSLETF152 FDSLVTQANI162 PNVFSMQMCG 172 AGGGSLVLGG191 IEPSLYKGDI201 WYTPIKEEWY211 YQIEILKLEI221 GGQSLNLDCR 231 EYNADKAIVD241 SGTTLLRLPQ251 KVFDAVVEAV261 ARASLIPEFS271 DGFWTGSQLA 281 CWTWSYFPKI296 SIYLRDENSS306 RSFRITILPQ316 LYIQPMYECY332 RFGISPSTNA 342 LVIGATVMEG352 FYVIFDRAQK362 RVGFAASPCA372 EIAGAAVSEI382 SGPFSTEDVA 392 SNCVPA
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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 .0BK or .0BK2 or .0BK3 or :30BK;style chemicals stick;color identity;select .A:27 or .A:28 or .A:29 or .A:30 or .A:46 or .A:48 or .A:49 or .A:50 or .A:51 or .A:85 or .A:87 or .A:88 or .A:89 or .A:92 or .A:124 or .A:126 or .A:129 or .A:131 or .A:134 or .A:142 or .A:170 or .A:211 or .A:239 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:344 or .A:347 or .A:351; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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GLY27
2.294
ARG28
3.008
GLY29
2.807
TYR30
3.517
LEU46
2.806
ASP48
1.946
THR49
5.000
GLY50
2.588
SER51
2.622
VAL85
4.845
TYR87
2.511
THR88
4.427
GLN89
4.944
TRP92
4.032
PHE124
2.419
LEU126
4.949
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Ligand Name: N-[3-[(4R,5R,6R)-2-azanyl-5-fluoranyl-4,6-dimethyl-5,6-dihydro-1,3-thiazin-4-yl]-4-fluoranyl-phenyl]-2,3-dihydro-[1,4]dioxino[2,3-c]pyridine-7-carboxamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 xaperone complex with N-{3-[(4R,5R,6R)-2-amino-5-fluoro-4,6-dimethyl-5,6-dihydro-4H-1,3-thiazin-4-yl]-4-fluorophenyl}-2H,3H-[1,4]dioxino[2,3-c]pyridine-7-carboxamide | PDB:7F1G | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.50 Å | Mutation | No | [5] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
ANFLAMVDNL
22 QGDGRGYYLE33 MLIGTPPQKL43 QILVDTGSSN53 FAVAGTPHSY63 IDTYFDTERS 73 STYRSKGFDV83 TVKYTQGSWT93 GFVGEDLVTI103 PKGFNTSFLV113 NIATIFESEN 123 FFLKWNGILG136 LAYATLAKPS146 SSLETFFDSL156 VTQANIPNVF166 SMQMCGANGG 185 SLVLGGIEPS195 LYKGDIWYTP205 IKEEWYYQIE215 ILKLEIGGQS225 LNLDCREYNA 235 DKAIVDSGTT245 LLRLPQKVFD255 AVVEAVARAS265 LIPEFSDGFW275 TGSQLACWTT 288 PWSYFPKISI298 YLRDENSSRS308 FRITILPQLY318 IQPMECYRFG335 ISPSTNALVI 345 GATVMEGFYV355 IFDRAQKRVG365 FAASPCAEIA375 GAAVSEISGP385 FSTEDVASNC 395 VP
|
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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 .0QQ or .0QQ2 or .0QQ3 or :30QQ;style chemicals stick;color identity;select .A:25 or .A:27 or .A:28 or .A:29 or .A:30 or .A:46 or .A:48 or .A:49 or .A:50 or .A:51 or .A:85 or .A:87 or .A:88 or .A:89 or .A:92 or .A:123 or .A:124 or .A:126 or .A:131 or .A:134 or .A:170 or .A:211 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:333 or .A:347 or .A:351; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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ASP25
2.566
GLY27
2.354
ARG28
2.957
GLY29
2.439
TYR30
2.754
LEU46
2.873
ASP48
1.875
THR49
4.969
GLY50
2.579
SER51
2.917
VAL85
4.723
TYR87
2.340
THR88
4.045
GLN89
4.326
TRP92
4.328
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Ligand Name: N-[3-[(5R)-3-azanyl-5-methyl-9,9-bis(oxidanylidene)-2,9$l^{6}-dithia-4-azaspiro[5.5]undec-3-en-5-yl]-4-fluoranyl-phenyl]-5-(fluoranylmethoxy)pyrazine-2-carboxamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 xaperone complex with N-{3-[(5R)-3-amino-5-methyl-9,9-dioxo-2,9lambda6-dithia-4-azaspiro[5.5]undec-3-en-5-yl]-4-fluorophenyl}-5-(fluoromethoxy)pyrazine-2-carboxamide | PDB:6JSZ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 1.53 Å | Mutation | No | [6] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
ANFLAMVDNL
22 QGGRGYYLEM34 LIGTPPQKLQ44 ILVDTGSSNF54 AVAGTPHSYI64 DTYFDTERSS 74 TYRSKGFDVT84 VKYTQGSWTG94 FVGEDLVTIP104 KGFNTSFLVN114 IATIFESENF 124 FLPGIKWNGI134 LGLAYATLAK144 PSSSLETFFD154 SLVTQANIPN164 VFSMQMCGAG 174 GGSLVLGGIE193 PSLYKGDIWY203 TPIKEEWYYQ213 IEILKLEIGG223 QSLNLDCREY 233 NADKAIVDSG243 TTLLRLPQKV253 FDAVVEAVAR263 ASLIPEFSDG273 FWTGSQLACW 283 WSYFPKISIY299 LRDENSSRSF309 RITILPQLYI319 QPMYECYRFG335 ISPSTNALVI 345 GATVMEGFYV355 IFDRAQKRVG365 FAASPCAEIA375 GAAVSEISGP385 FSTEDVASNC 395 VPA
|
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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 .C7O or .C7O2 or .C7O3 or :3C7O;style chemicals stick;color identity;select .A:27 or .A:28 or .A:29 or .A:30 or .A:46 or .A:48 or .A:50 or .A:51 or .A:85 or .A:86 or .A:87 or .A:124 or .A:131 or .A:134 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:347; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: 5-(2,2,2-Trifluoro-Ethoxy)-Pyridine-2-Carboxylic Acid [3-((S)-2-Amino-1,4-Dimethyl-6-Oxo-1,4,5,6-Tetrahydro-Pyrimidin-4-Yl)-Phenyl]-Amide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 FAB INHIBITOR COMPLEX | PDB:3ZKN | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [7] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
NFLAMVDNLQ
23 GDSGRGYYLE33 MLIGTPPQKL43 QILVDTGSSN53 FAVAGTPHSY63 IDTYFDTERS 73 STYRSKGFDV83 TVKYTQGSWT93 GFVGEDLVTI103 PKGFNTSFLV113 NIATIFESEN 123 FFLPGIKWNG133 ILGLAYATLA143 KPSSSLETFF153 DSLVTQANIP163 NVFSMQMCGA 173 NGGSLVLGGI192 EPSLYKGDIW202 YTPIKEEWYY212 QIEILKLEIG222 GQSLNLDCRE 232 YNADKAIVDS242 GTTLLRLPQK252 VFDAVVEAVA262 RASLIPEFSD272 GFWTGSQLAC 282 WTNSETPWSY292 FPKISIYLRD302 ENSSRSFRIT312 ILPQLYIQPM322 MGAGLNYECY 332 RFGISPSTNA342 LVIGATVMEG352 FYVIFDRAQK362 RVGFAASPCA372 EIAGAAVSEI 382 SGPFSTEDVA392 SNCVP
|
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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 .WZV or .WZV2 or .WZV3 or :3WZV;style chemicals stick;color identity;select .A:46 or .A:48 or .A:50 or .A:51 or .A:85 or .A:87 or .A:89 or .A:90 or .A:123 or .A:124 or .A:126 or .A:131 or .A:134 or .A:241 or .A:243 or .A:244; 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-[(9S)-7-azanyl-2,2-bis(fluoranyl)-9-prop-1-ynyl-6-oxa-8-azaspiro[3.5]non-7-en-9-yl]-4-fluoranyl-phenyl]-5-cyano-pyridine-2-carboxamide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 xaperone complex with N-{3-[(9S)-7-amino-2,2-difluoro-9-(prop-1-yn-1-yl)-6-oxa-8-azaspiro[3.5]non-7-en-9-yl]-4-fluorophenyl}-5-cyanopyridine-2-carboxamide | PDB:7D5U | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.04 Å | Mutation | No | [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
FLAMVDNLQG
24 DSGRGYYLEM34 LIGTPPQKLQ44 ILVDTGSSNF54 AVAGTPHSYI64 DTYFDTERSS 74 TYRSKGFDVT84 VKYTQGSWTG94 FVGEDLVTIP104 KGFNTSFLVN114 IATIFESENF 124 FLPGIKWNGI134 LGLAYATLAK144 PSSSLETFFD154 SLVTQANIPN164 VFSMQMCGAN 183 GGSLVLGGIE193 PSLYKGDIWY203 TPIKEEWYYQ213 IEILKLEIGG223 QSLNLDCREY 233 NADKAIVDSG243 TTLLRLPQKV253 FDAVVEAVAR263 ASLIPEFSDG273 FWTGSQLACW 283 TNSETPWSYF293 PKISIYLRDE303 NSSRSFRITI313 LPQLYIQPML327 NYECYRFGIS 337 PSTNALVIGA347 TVMEGFYVIF357 DRAQKRVGFA367 ASPCAEIAGA377 AVSEISGPFS 387 TEDVASNCVP397
|
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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 .GX6 or .GX62 or .GX63 or :3GX6;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:46 or .A:48 or .A:50 or .A:51 or .A:85 or .A:87 or .A:92 or .A:123 or .A:124 or .A:129 or .A:131 or .A:134 or .A:170 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:347; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP25
3.769
SER26
3.026
GLY27
3.767
ARG28
4.346
GLY29
3.594
TYR30
3.756
LEU46
3.671
ASP48
2.601
GLY50
3.596
SER51
3.823
VAL85
3.940
TYR87
3.028
TRP92
3.464
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Ligand Name: 5-Ethoxy-Pyridine-2-Carboxylic Acid [3-((R)-2-Amino-5,5-Difluoro-4-Methyl-5,6-Dihydro-4h-[1,3]oxazin-4-Yl)-4-Fluoro-Phenyl]-Amide | Ligand Info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure Description | BACE2 XAPERONE COMPLEX | PDB:3ZLQ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [8] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
PDB Sequence |
LAMVDNLQGD
25 SGRGYYLEML35 IGTPPQKLQI45 LVDTGSSNFA55 VAGTPHSYID65 TYFDTERSST 75 YRSKGFDVTV85 KYTQGSWTGF95 VGEDLVTIPK105 GFNTSFLVNI115 ATIFESENFF 125 LPGIKWNGIL135 GLAYATLAKP145 SSSLETFFDS155 LVTQANIPNV165 FSMQMCGAGG 184 GSLVLGGIEP194 SLYKGDIWYT204 PIKEEWYYQI214 EILKLEIGGQ224 SLNLDCREYN 234 ADKAIVDSGT244 TLLRLPQKVF254 DAVVEAVARA264 SDGFWTGSQL280 ACWTNSETPW 290 SYFPKISIYL300 RDENSSRSFR310 ITILPQLYIQ320 PMMGAGLNYE330 CYRFGISPST 340 NALVIGATVM350 EGFYVIFDRA360 QKRVGFAASP370 CAEIAGAAVS380 EISGPFSTED 390 VASNCVP
|
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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 .6T9 or .6T92 or .6T93 or :36T9;style chemicals stick;color identity;select .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:46 or .A:48 or .A:50 or .A:51 or .A:87 or .A:89 or .A:92 or .A:124 or .A:131 or .A:134 or .A:170 or .A:241 or .A:242 or .A:243 or .A:244 or .A:245 or .A:347; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP25
4.116
SER26
3.397
GLY27
3.542
ARG28
3.701
GLY29
3.130
TYR30
3.705
LEU46
3.453
ASP48
2.581
GLY50
3.870
SER51
3.787
TYR87
3.381
GLN89
4.952
|
References | Top | ||||
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REF 1 | Structure-Based Approaches to Improving Selectivity through Utilizing Explicit Water Molecules: Discovery of Selective beta-Secretase (BACE1) Inhibitors over BACE2. J Med Chem. 2021 Mar 25;64(6):3075-3085. | ||||
REF 2 | Crystal structure of human BACE2 in complex with a hydroxyethylamine transition-state inhibitor. J Mol Biol. 2006 Jan 13;355(2):249-61. | ||||
REF 3 | A Structure-Based Discovery Platform for BACE2 and the Development of Selective BACE Inhibitors. ACS Chem Neurosci. 2021 Feb 17;12(4):581-588. | ||||
REF 4 | JNJ-67569762, A 2-Aminotetrahydropyridine-Based Selective BACE1 Inhibitor Targeting the S3 Pocket: From Discovery to Clinical Candidate. J Med Chem. 2021 Oct 14;64(19):14175-14191. | ||||
REF 5 | Discovery of Extremely Selective Fused Pyridine-Derived beta-Site Amyloid Precursor Protein-Cleaving Enzyme (BACE1) Inhibitors with High In Vivo Efficacy through 10s Loop Interactions. J Med Chem. 2021 Oct 14;64(19):14165-14174. | ||||
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