Structure of PDB 2py3 Chain A Binding Site BS01

Receptor Information
>2py3 Chain A (length=282) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPEDPKWEFPRDKLTLGKPLFGQVVMAEAVGIDKDKPKEAVTVAVKMLKD
DATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVGYASKGN
LREYLRARRPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV
TENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQS
DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYM
MMRDCWHAVPSQRPTFKQLVEDLDRILTLTTN
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2py3 Chain A Residue 803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2py3 A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		N631 D644
Binding residue
(residue number reindexed from 1)		N147 D160
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D626 A628 R630 N631 D644 R664
Catalytic site (residue number reindexed from 1) D142 A144 R146 N147 D160 R180
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
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:2py3, PDBe:2py3, PDBj:2py3
PDBsum2py3
PubMed17803937
UniProtP21802|FGFR2_HUMAN Fibroblast growth factor receptor 2 (Gene Name=FGFR2)

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