Structure of PDB 3poz Chain A

Receptor sequence
>3pozA (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
QALLRILKETEFKKIKVLGSGAFGTVYKGLWIPVKIPVAIKELANKEILD
EAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGS
QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKL
LGAEEKKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGI
PASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEF
SKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDVVDADEYL
3D structure
PDB3poz Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein.
ChainA
Resolution1.5 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 03P A V726 A743 K745 M766 C775 R776 L788 T790 M793 L844 T854 D855 F856 V26 A39 K41 M55 C64 R65 L77 T79 M82 L133 T143 D144 F145 MOAD: ic50=23nM
PDBbind-CN: -logKd/Ki=7.64,IC50=23nM
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:3poz, PDBe:3poz, PDBj:3poz
PDBsum3poz
PubMed21454582
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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