Structure of PDB 2ity Chain A

Receptor sequence
>2ityA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFG
CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK
TPQHVKITDFGLAKLLGAEVPIKWMALESILHRIYTHQSDVWSYGVTVWE
LMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDAD
SRPKFRELIIEFSKMARDPQRYLVIQGDERMHLDEEDMDDVVDADEYLIP
3D structure
PDB2ity Structures of Lung Cancer-Derived Egfr Mutants and Inhibitor Complexes: Mechanism of Activation and Insights Into Differential Inhibitor Sensitivity
ChainA
Resolution3.42 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
Catalytic site (residue number reindexed from 1) D141 A143 R145 N146 D159
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 IRE A L718 A743 L788 T790 L792 M793 G796 L844 L22 A47 L92 T94 L96 M97 G100 L148 PDBbind-CN: -logKd/Ki=7.27,Kd=53.5nM
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:2ity, PDBe:2ity, PDBj:2ity
PDBsum2ity
PubMed17349580
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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