Structure of PDB 4rix Chain C Binding Site BS02

Receptor Information
>4rix Chain C (length=275) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIESFQ
AVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRG
ALGPRLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFG
VADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEL
MTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENI
RPTFKELANEFTRMARDPPRYLVIK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4rix Chain C Residue 1102 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4rix Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		N820 D833
Binding residue
(residue number reindexed from 1)		N135 D148
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N815 A817 R819 N820 D833 D843 T854
Catalytic site (residue number reindexed from 1) N130 A132 R134 N135 D148 D158 T169
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4rix, PDBe:4rix, PDBj:4rix
PDBsum4rix
PubMed25468994
UniProtP21860|ERBB3_HUMAN Receptor tyrosine-protein kinase erbB-3 (Gene Name=ERBB3)

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