Structure of PDB 3lmg Chain B Binding Site BS01

Receptor Information

>3lmg Chain B (length=268) Species: 9606 (Homo sapiens)

VLARIFKETELRKLKVLGSGVFGTVHKGVWIPGESIKIPVCIKVIEDKSQ
SFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQ
HRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVA
DFGVADLLPPDDKPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAE
PYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKE
LANEFTRMARDPPRYLVI

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 3lmg Chain B Residue 202

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3lmg ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation.
• Resolution: 2.8 Å
• Binding residue (original residue number in PDB): N820 D833
• Binding residue (residue number reindexed from 1): N138 D151
• Annotation score: 1

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.

Gene Ontology

Molecular Function

• GO:0004672 protein kinase activity
• GO:0005524 ATP binding

Biological Process

• GO:0006468 protein phosphorylation

External links

• PDB: RCSB:3lmg, PDBe:3lmg, PDBj:3lmg
• PDBsum: 3lmg
• PubMed: 20351256
• UniProt: P21860|ERBB3_HUMAN Receptor tyrosine-protein kinase erbB-3 (Gene Name=ERBB3)