Structure of PDB 3vs2 Chain B

Receptor sequence
>3vs2B (length=434) Species: 9606 (Homo sapiens) [Search protein sequence]
RIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIP
SNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGS
YSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKG
NDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMA
TYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPI
YIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIH
RDLRAANILVSASLVCKIADFGLARVIPIKWTAPEAINFGSFTIKSDVWS
FGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMR
CWKNRPEERPTFEYIQSVLDDFYTATESQYEEIP
3D structure
PDB3vs2 A Pyrrolo-Pyrimidine Derivative Targets Human Primary AML Stem Cells in Vivo
ChainB
Resolution2.609 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D386 R388 A390 N391 D404
Catalytic site (residue number reindexed from 1) D302 R304 A306 N307 D320
Enzyme Commision number 2.7.10.2: non-specific 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 CA B E524 Y527 E529 E427 Y430 E432
BS02 VSB B V281 A293 K295 L325 T338 M341 S345 L393 A403 D404 F405 V197 A209 K211 L241 T254 M257 S261 L309 A319 D320 F321
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase 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:3vs2, PDBe:3vs2, PDBj:3vs2
PDBsum3vs2
PubMed23596204
UniProtP08631|HCK_HUMAN Tyrosine-protein kinase HCK (Gene Name=HCK)

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