Structure of PDB 4xuf Chain B

Receptor sequence
>4xufB (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
DLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEK
ADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDL
LNYLRSKRNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHG
KVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVW
SYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIM
QSCWAFDSRKRPSFPNLTSFLGCQ
3D structure
PDB4xuf Crystal Structure of the FLT3 Kinase Domain Bound to the Inhibitor Quizartinib (AC220).
ChainB
Resolution3.2 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 A813 R815 N816 D829
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 P30 B L616 E661 M664 M665 I674 Y693 C694 C695 G697 H809 L818 C828 D829 F830 L17 E62 M65 M66 I75 Y94 C95 C96 G98 H137 L146 C156 D157 F158 BindingDB: Kd=1.6nM,IC50=69nM
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:4xuf, PDBe:4xuf, PDBj:4xuf
PDBsum4xuf
PubMed25837374
UniProtP36888|FLT3_HUMAN Receptor-type tyrosine-protein kinase FLT3 (Gene Name=FLT3)

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