Target Binding Site Detail
Target General Information | Top | ||||
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Target ID | T86350 | Target Info | |||
Target Name | Erbb3 tyrosine kinase receptor (Erbb-3) | ||||
Synonyms | Tyrosine kinase-type cell surface receptor HER3; Receptor tyrosine-protein kinase erbB-3; Proto-oncogene-like protein c-ErbB-3; HER3; C-erbB3; C-erbB-3 protein | ||||
Target Type | Clinical trial Target | ||||
Gene Name | ERBB3 | ||||
Biochemical Class | Kinase | ||||
UniProt ID |
Ligand General Information | Top | ||||
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Ligand Name | AMP-PNP | Ligand Info | |||
Canonical SMILES | C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N | ||||
InChI | 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1 | ||||
InChIKey | PVKSNHVPLWYQGJ-KQYNXXCUSA-N | ||||
PubChem Compound ID | 33113 |
Drug Binding Sites of Target | Top | |||||
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PDB ID: 3LMG Crystal structure of the ERBB3 kinase domain in complex with AMP-PNP | ||||||
Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [1] |
PDB Sequence |
VLARIFKETE
689 LRKLKVLGSG699 VFGTVHKGVW709 IPEGESIKIP719 VCIKVIEDKQ732 SFQAVTDHML 742 AIGSLDHAHI752 VRLLGLCPGS762 SLQLVTQYLP772 LGSLLDHVRQ782 HRGALGPQLL 792 LNWGVQIAKG802 MYYLEEHGMV812 HRNLAARNVL822 LKSPSQVQVA832 DFGVADLLPP 842 DDTPIKWMAL861 ESIHFGKYTH871 QSDVWSYGVT881 VWELMTFGAE891 PYAGLRLAEV 901 PDLLEKGERL911 AQPQICTIDV921 YMVMVKCWMI931 DENIRPTFKE941 LANEFTRMAR 951 DPPRYLVI
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LEU696
3.564
GLY697
3.741
SER698
3.635
GLY699
2.875
VAL700
2.879
PHE701
4.382
GLY702
3.570
THR703
4.381
VAL704
3.149
CYS721
3.471
LYS723
2.901
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PDB ID: 4RIY Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-E909G mutation | ||||||
Method | X-ray diffraction | Resolution | 2.98 Å | Mutation | Yes | [2] |
PDB Sequence |
VLARIFKETE
689 LRKLKVLGSG699 VFGTVHKGVW709 IPEGESIKIP719 VCIKVIEDKS729 GRQSFQAVTD 739 HMLAIGSLDH749 AHIVRLLGLC759 PGSSLQLVTQ769 YLPLGSLLDH779 VRQHRGALGP 789 QLLLNWGVQI799 AKGMYYLEEH809 GMVHRNLAAR819 NVLLKSPSQV829 QVADFGVADL 839 LPPPIKWMAL861 ESIHFGKYTH871 QSDVWSYGVT881 VWELMTFGAE891 PYAGLRLAEV 901 PDLLEKGGRL911 AQPQICTIDV921 YMVMVKCWMI931 DENIRPTFKE941 LANEFTRMAR 951 DPPRYLVIK
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LEU696
3.770
GLY697
3.586
SER698
3.169
GLY699
2.872
VAL700
3.329
PHE701
4.622
GLY702
4.234
VAL704
3.308
CYS721
3.603
LYS723
2.925
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PDB ID: 4RIW Crystal structure of an EGFR/HER3 kinase domain heterodimer | ||||||
Method | X-ray diffraction | Resolution | 3.10 Å | Mutation | Yes | [2] |
PDB Sequence |
VLARIFKETE
689 LRKLKVLGSG699 VFGTVHKGVW709 IPEGESIKIP719 VCIKVIEDKS729 GRQSFQAVTD 739 HMLAIGSLDH749 AHIVRLLGLC759 PGSSLQLVTQ769 YLPLGSLLDH779 VRQHRGALGP 789 QLLLNWGVQI799 AKGMYYLEEH809 GMVHRNLAAR819 NVLLKSPSQV829 QVADFGVADL 839 LPPPIKWMAL861 ESIHFGKYTH871 QSDVWSYGVT881 VWELMTFGAE891 PYAGLRLAEV 901 PDLLEKGERL911 AQPQICTIDV921 YMVMVKCWMI931 DENIRPTFKE941 LANEFTRMAR 951 DPPRYLVIK
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LEU696
3.993
GLY697
3.580
SER698
3.059
GLY699
2.688
VAL700
3.436
PHE701
4.711
GLY702
4.209
VAL704
3.262
CYS721
3.656
LYS723
3.362
VAL753
4.977
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PDB ID: 4RIX Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-Q790R mutation | ||||||
Method | X-ray diffraction | Resolution | 3.10 Å | Mutation | Yes | [2] |
PDB Sequence |
VLARIFKETE
689 LRKLKVLGSG699 VFGTVHKGVW709 IPEGESIKIP719 VCIKVIEDKS729 GRQSFQAVTD 739 HMLAIGSLDH749 AHIVRLLGLC759 PGSSLQLVTQ769 YLPLGSLLDH779 VRQHRGALGP 789 RLLLNWGVQI799 AKGMYYLEEH809 GMVHRNLAAR819 NVLLKSPSQV829 QVADFGVADL 839 LPPPIKWMAL861 ESIHFGKYTH871 QSDVWSYGVT881 VWELMTFGAE891 PYAGLRLAEV 901 PDLLEKGERL911 AQPQICTIDV921 YMVMVKCWMI931 DENIRPTFKE941 LANEFTRMAR 951 DPPRYLVIK
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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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:696 or .A:697 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:704 or .A:721 or .A:723 or .A:753 or .A:768 or .A:769 or .A:770 or .A:771 or .A:775 or .A:815 or .A:819 or .A:820 or .A:822 or .A:833; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU696
3.652
GLY697
3.558
SER698
2.986
GLY699
2.764
VAL700
3.462
PHE701
4.768
GLY702
4.166
VAL704
3.313
CYS721
3.704
LYS723
3.166
VAL753
4.963
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PDB ID: 3KEX Crystal structure of the catalytically inactive kinase domain of the human epidermal growth factor receptor 3 (HER3) | ||||||
Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [3] |
PDB Sequence |
KVLARIFKET
688 ELRKLKVLGS698 GVFGTVHKGV708 WIPEGESIKI718 PVCIKVIEDK728 SGRQSFQAVT 738 DHMLAIGSLD748 HAHIVRLLGL758 CPGSSLQLVT768 QYLPLGSLLD778 HVRQHRGALG 788 PQLLLNWGVQ798 IAKGMYYLEE808 HGMVHRNLAA818 RNVLLKSPSQ828 VQVADFGVAD 838 LLPPDDKQLL848 TPIKWMALES863 IHFGKYTHQS873 DVWSYGVTVW883 ELMTFGAEPY 893 AGLRLAEVPD903 LLEKGERLAQ913 PQICTIDVYM923 VMVKCWMIDE933 NIRPTFKELA 943 NEFTRMARDP953 PRYLVIKRES963 GPGIAPGPEP973 HG
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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 .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:696 or .A:697 or .A:698 or .A:699 or .A:700 or .A:701 or .A:702 or .A:704 or .A:721 or .A:723 or .A:753 or .A:768 or .A:769 or .A:770 or .A:771 or .A:772 or .A:774 or .A:775 or .A:815 or .A:819 or .A:820 or .A:822 or .A:833; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LEU696
3.380
GLY697
3.065
SER698
2.898
GLY699
2.888
VAL700
3.035
PHE701
4.817
GLY702
3.614
VAL704
3.085
CYS721
3.563
LYS723
3.484
VAL753
4.334
THR768
3.897
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References | Top | ||||
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REF 1 | ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc Natl Acad Sci U S A. 2010 Apr 27;107(17):7692-7. | ||||
REF 2 | Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations. Sci Signal. 2014 Dec 2;7(354):ra114. | ||||
REF 3 | Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21608-13. |
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