Structure of PDB 1oec Chain A

Receptor sequence
>1oecA (length=280) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIKPKEAVTVAVKML
KDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASK
GNLREYLRARREQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV
TENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS
DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYM
MMRDCWHAVPSQRPTFKQLVEDLDRILTLT
3D structure
PDB1oec The Crystal Structure of the Fgfr2 Tyrosine Kinase Domain in Complex with 4-Aryl-2-Phenylamino Pyrimidine Angiogenesis Inhibitors
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D626 A628 R630 N631 D644
Catalytic site (residue number reindexed from 1) D142 A144 R146 N147 D160
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 AA2 A G490 A567 L633 D644 G24 A98 L149 D160
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
View graph for
Biological Process
External links
PDB RCSB:1oec, PDBe:1oec, PDBj:1oec
PDBsum1oec
PubMed
UniProtP21802|FGFR2_HUMAN Fibroblast growth factor receptor 2 (Gene Name=FGFR2)

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