Structure of PDB 5vnd Chain A

Receptor sequence
>5vndA (length=302) Species: 9606 (Homo sapiens) [Search protein sequence]
YELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKDKPNRVTKVA
VKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVE
CASKGNLREYLQARRPPGLEYSYNPSHNPEEQLSSKDLVSCAYQVARGME
YLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDHHIDYYKKTTNGRLP
VKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLL
KEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSN
QE
3D structure
PDB5vnd H3B-6527 Is a Potent and Selective Inhibitor of FGFR4 in FGF19-Driven Hepatocellular Carcinoma.
ChainA
Resolution2.2 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) D161 A163 R165 N166 D179
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 9ES A V492 L494 A512 K514 E531 I545 V561 C563 A564 G567 E571 L630 A640 D641 V30 L32 A50 K52 E69 I83 V99 C101 A102 G105 E109 L168 A178 D179 PDBbind-CN: -logKd/Ki=6.49,IC50=320nM
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:5vnd, PDBe:5vnd, PDBj:5vnd
PDBsum5vnd
PubMed29247039
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

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