Structure of PDB 4f65 Chain A

Receptor sequence
>4f65A (length=279) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKPNRVTKVAVKM
LKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYAS
KGNLREYLQARRPPPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAA
RNVLVTEDNVMKIADFYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSF
GVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDC
WHAVPSQRPTFKQLVEDLDRIVALTSNQE
3D structure
PDB4f65 Protein-Ligand Crystal Structures Can Guide the Design of Selective Inhibitors of the FGFR Tyrosine Kinase.
ChainA
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D623 A625 R627 N628 D641
Catalytic site (residue number reindexed from 1) D147 A149 R151 N152 D165
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 0S9 A L484 E486 V492 A512 K514 E531 V561 Y563 A564 S565 G567 L630 L21 E23 V29 A47 K49 E66 V96 Y98 A99 S100 G102 L154 MOAD: ic50=2.5nM
PDBbind-CN: -logKd/Ki=8.60,IC50=2.5nM
BindingDB: IC50=63.1nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005007 fibroblast growth factor receptor 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:4f65, PDBe:4f65, PDBj:4f65
PDBsum4f65
PubMed22612866
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

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