Structure of PDB 6jqr Chain A

Receptor sequence
>6jqrA (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
RYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGA
FGKVMNATAYGISVSIQVAVKMLKEDSSEREALMSELKMMTQLGSHENIV
NLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFSNVLTFEDLLCFAYQ
VAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFMSDSNYVVRGNARL
PVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYK
LIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADA
E
3D structure
PDB6jqr Effect of Fms-like tyrosine kinase 3 (FLT3) ligand (FL) on antitumor activity of gilteritinib, a FLT3 inhibitor, in mice xenografted with FL-overexpressing cells.
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) D811 R815 N816 D829
Catalytic site (residue number reindexed from 1) D167 R171 N172 D185
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 C6F A L616 A642 Y693 C694 G697 L818 L46 A69 Y118 C119 G122 L174 BindingDB: IC50=0.41nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004714 transmembrane receptor protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:6jqr, PDBe:6jqr, PDBj:6jqr
PDBsum6jqr
PubMed31692922
UniProtP36888|FLT3_HUMAN Receptor-type tyrosine-protein kinase FLT3 (Gene Name=FLT3)

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