Structure of PDB 2j6m Chain A

Receptor sequence
>2j6mA (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFG
CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK
TPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSD
VWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMI
MVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDDEEDMDDVVDAD
EYLIPQ
3D structure
PDB2j6m Structures of Lung Cancer-Derived Egfr Mutants and Inhibitor Complexes: Mechanism of Activation and Insights Into Differential Inhibitor Sensitivity
ChainA
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D837 A839 R841 N842 D855 G874
Catalytic site (residue number reindexed from 1) D141 A143 R145 N146 D159 G178
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 AEE A A743 T790 M793 P794 G796 E804 L844 A47 T94 M97 P98 G100 E108 L148 PDBbind-CN: -logKd/Ki=7.96,Kd=10.9nM
BindingDB: Kd=5.3nM,IC50=2nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine 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:2j6m, PDBe:2j6m, PDBj:2j6m
PDBsum2j6m
PubMed17349580
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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