Structure of PDB 4riy Chain A

Receptor sequence
>4riyA (length=269) Species: 9606 (Homo sapiens) [Search protein sequence]
VLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKS
GRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDH
VRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQV
QVADFGVADLLPPPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAE
PYAGLRLAEVPDLLEKGGRLAQPQICTIDVYMVMVKCWMIDENIRPTFKE
LANEFTRMARDPPRYLVIK
3D structure
PDB4riy Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
ChainA
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
Catalytic site (residue number reindexed from 1) N136 A138 R140 N141 D154
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 A G697 G699 V700 V704 C721 K723 L771 N815 R819 N820 L822 D833 G18 G20 V21 V25 C42 K44 L92 N136 R140 N141 L143 D154
BS02 MG A N820 D833 N141 D154
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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