Structure of PDB 5x02 Chain A

Receptor sequence
>5x02A (length=305) Species: 9606 (Homo sapiens) [Search protein sequence]
ESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFG
KVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHE
NIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFSVLTFEDLLCFA
YQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNY
VVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGI
PVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSF
LGCQL
3D structure
PDB5x02 A novel irreversible FLT3 inhibitor, FF-10101, shows excellent efficacy against AML cells withFLT3mutations.
ChainA
Resolution2.401 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) D169 R173 N174 D187
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 F6M A L616 V624 A642 K644 V675 F691 E692 Y693 C694 C695 Y696 L818 C828 F830 L44 V52 A70 K72 V103 F119 E120 Y121 C122 C123 Y124 L176 C186 F188 PDBbind-CN: -logKd/Ki=9.85,IC50=0.14nM
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:5x02, PDBe:5x02, PDBj:5x02
PDBsum5x02
PubMed29187377
UniProtP36888|FLT3_HUMAN Receptor-type tyrosine-protein kinase FLT3 (Gene Name=FLT3)

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