Structure of PDB 2hk5 Chain A

Receptor sequence
>2hk5A (length=269) Species: 9606 (Homo sapiens) [Search protein sequence]
AQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPG
SMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFL
KSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVC
KIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGI
LLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWK
NRPEERPTFEYIQSVLDDF
3D structure
PDB2hk5 The development of 2-benzimidazole substituted pyrimidine based inhibitors of lymphocyte specific kinase (Lck).
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D364 R366 A368 N369 D382 F402
Catalytic site (residue number reindexed from 1) D136 R138 A140 N141 D154 F174
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 1BM A L251 A271 K273 E288 I314 T316 F318 M319 G322 A368 N369 L371 D382 L23 A43 K45 E60 I86 T88 F90 M91 G94 A140 N141 L143 D154 MOAD: ic50=46nM
PDBbind-CN: -logKd/Ki=7.34,IC50=46nM
BindingDB: IC50=46nM
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:2hk5, PDBe:2hk5, PDBj:2hk5
PDBsum2hk5
PubMed16997556
UniProtP08631|HCK_HUMAN Tyrosine-protein kinase HCK (Gene Name=HCK)

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