Structure of PDB 3bel Chain A

Receptor sequence
>3belA (length=280) Species: 9606 (Homo sapiens) [Search protein sequence]
ALLRILKETEFKKIKVLGSGAFGTVYKGLWIPVKIPVAIKELKANKEILD
EAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGS
QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKL
LGAEEKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIP
ASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFS
KMARDPQRYLVIQGDERNFYRALMVVDADE
3D structure
PDB3bel Discovery of novel 4-amino-6-arylaminopyrimidine-5-carbaldehyde oximes as dual inhibitors of EGFR and ErbB-2 protein tyrosine kinases.
ChainA
Resolution2.3 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) D126 A128 R130 N131 D144
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 POX A A743 K745 C775 R776 L788 T790 M793 D800 L844 T854 D855 F856 A38 K40 C64 R65 L77 T79 M82 D89 L133 T143 D144 F145 MOAD: ic50=0.014uM
PDBbind-CN: -logKd/Ki=7.85,IC50=0.014uM
BindingDB: IC50=14nM
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:3bel, PDBe:3bel, PDBj:3bel
PDBsum3bel
PubMed18508264
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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