Structure of PDB 4jrv Chain A

Receptor sequence
>4jrvA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIK
ELTSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCL
LDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTP
QHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVW
SYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMV
KCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDDMDDVVDADEYLIP
3D structure
PDB4jrv Protein Kinase Inhibitor Design by Targeting the Asp-Phe-Gly (DFG) Motif: The Role of the DFG Motif in the Design of Epidermal Growth Factor Receptor Inhibitors
ChainA
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) D813 A815 R817 N818 D831 G850
Catalytic site (residue number reindexed from 1) D139 A141 R143 N144 D157 G176
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 KJV A L694 V702 A719 K721 T766 Q767 M769 G772 N818 L820 D831 L23 V31 A48 K50 T92 Q93 M95 G98 N144 L146 D157 PDBbind-CN: -logKd/Ki=7.54,IC50=29nM
BindingDB: IC50=29nM
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:4jrv, PDBe:4jrv, PDBj:4jrv
PDBsum4jrv
PubMed23611691
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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