Structure of PDB 3vs2 Chain A

Receptor sequence
>3vs2A (length=431) Species: 9606 (Homo sapiens) [Search protein sequence]
RIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIP
SNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGS
YSLSVRDYDPRQGDTVKHYKIRTLGFYISPRSTFSTLQELVDHYKKGNDG
LCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYN
KHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYII
TEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDL
RAANILVSASLVCKIADFGLARVIPIKWTAPEAINFGSFTIKSDVWSFGI
LLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWK
NRPEERPTFEYIQSVLDDFYTATESQYEEIP
3D structure
PDB3vs2 A Pyrrolo-Pyrimidine Derivative Targets Human Primary AML Stem Cells in Vivo
ChainA
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) D299 R301 A303 N304 D317
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 VSB A L273 V281 A293 K295 V323 T338 M341 S345 L393 D404 F405 L186 V194 A206 K208 V236 T251 M254 S258 L306 D317 F318
BS02 CA A E524 Y527 E528 E529 E424 Y427 E428 E429
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

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Molecular Function
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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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