Structure of PDB 3lmg Chain B

Receptor sequence
>3lmgB (length=268) Species: 9606 (Homo sapiens) [Search protein sequence]
VLARIFKETELRKLKVLGSGVFGTVHKGVWIPGESIKIPVCIKVIEDKSQ
SFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQ
HRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVA
DFGVADLLPPDDKPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAE
PYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKE
LANEFTRMARDPPRYLVI
3D structure
PDB3lmg ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation.
ChainB
Resolution2.8 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) N133 A135 R137 N138 D151
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 MG B N820 D833 N138 D151
BS02 ANP B G697 S698 G699 V704 C721 K723 Q769 Y770 L771 R819 N820 L822 D833 G18 S19 G20 V25 C41 K43 Q87 Y88 L89 R137 N138 L140 D151
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:3lmg, PDBe:3lmg, PDBj:3lmg
PDBsum3lmg
PubMed20351256
UniProtP21860|ERBB3_HUMAN Receptor tyrosine-protein kinase erbB-3 (Gene Name=ERBB3)

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