Structure of PDB 4riy Chain C

Receptor sequence
>4riyC (length=275) Species: 9606 (Homo sapiens) [Search protein sequence]
VLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIESFQ
AVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRG
ALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFG
VADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEL
MTFGAEPYAGLRLAEVPDLLEKGGRLAQPQICTIDVYMVMVKCWMIDENI
RPTFKELANEFTRMARDPPRYLVIK
3D structure
PDB4riy Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
ChainC
Resolution2.981 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ANP C G697 G699 V700 V704 C721 K723 L771 N815 R819 N820 L822 D833 G18 G20 V21 V25 C42 K44 L86 N130 R134 N135 L137 D148
BS02 MG C N820 D833 N135 D148
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:4riy, PDBe:4riy, PDBj:4riy
PDBsum4riy
PubMed25468994
UniProtP21860|ERBB3_HUMAN Receptor tyrosine-protein kinase erbB-3 (Gene Name=ERBB3)

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