Structure of PDB 3w2o Chain A

Receptor sequence
>3w2oA (length=305) Species: 9606 (Homo sapiens) [Search protein sequence]
HAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFG
CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK
TPQHVKITDFGRAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSD
VWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMI
MVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPMDDVVD
ADEYL
3D structure
PDB3w2o Structure-Based Approach for the Discovery of Pyrrolo[3,2-d]pyrimidine-Based EGFR T790M/L858R Mutant Inhibitors.
ChainA
Resolution2.35 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 03P A S720 G721 V726 A743 K745 E762 M766 L788 M790 M793 S24 G25 V30 A47 K49 E66 M70 L92 M94 M97 PDBbind-CN: -logKd/Ki=5.08,IC50=8400nM
BindingDB: IC50=4.0nM
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:3w2o, PDBe:3w2o, PDBj:3w2o
PDBsum3w2o
PubMed24900643
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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