Structure of PDB 4f64 Chain B

Receptor sequence
>4f64B (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
SEYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLPNRVTKVAVK
MLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYA
SKGNLREYLQARRQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVL
VTEDNVMKIADFGLADYYKKGRLPVKWMAPEALFDRIYTHQSDVWSFGVL
LWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHA
VPSQRPTFKQLVEDLDRIVALT
3D structure
PDB4f64 Protein-Ligand Crystal Structures Can Guide the Design of Selective Inhibitors of the FGFR Tyrosine Kinase.
ChainB
Resolution2.05 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) D143 A145 R147 N148 D161
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 0S8 B L484 A512 V561 A564 S565 G567 L630 L24 A48 V97 A100 S101 G103 L150 MOAD: ic50=63nM
BindingDB: IC50=794.33nM
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:4f64, PDBe:4f64, PDBj:4f64
PDBsum4f64
PubMed22612866
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

[Back to BioLiP]