Structure of PDB 4f63 Chain A

Receptor sequence
>4f63A (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPEDPRWELPRDRLVLGKPLGQVVLAEAIGLPNRVTKVAVKMLKSDATE
KDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREY
LQARRPPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED
NVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVW
SFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMR
DCWHAVPSQRPTFKQLVEDLDRIVALTS
3D structure
PDB4f63 Protein-Ligand Crystal Structures Can Guide the Design of Selective Inhibitors of the FGFR Tyrosine Kinase.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D623 A625 R627 N628 D641
Catalytic site (residue number reindexed from 1) D139 A141 R143 N144 D157
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 0S7 A L484 A512 Y563 A564 S565 G567 L630 L21 A40 Y91 A92 S93 G95 L146 PDBbind-CN: -logKd/Ki=6.30,IC50=0.5uM
BindingDB: IC50=501.19nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4f63, PDBe:4f63, PDBj:4f63
PDBsum4f63
PubMed22612866
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

[Back to BioLiP]