Structure of PDB 2hy0 Chain A

Receptor sequence
>2hy0A (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
AVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKNIKKEICI
NKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQ
RFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYN
NRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPW
DQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPD
IKKDRWYNKPLKKGAKRPRVTS
3D structure
PDB2hy0 Development of 6-substituted indolylquinolinones as potent Chek1 kinase inhibitors.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D130 K132 E134 N135 D148 T170
Catalytic site (residue number reindexed from 1) D122 K124 E126 N127 D140 T162
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 306 A Q13 L15 V23 A36 K38 E85 Y86 C87 G90 L137 D148 Q12 L14 V22 A35 K37 E77 Y78 C79 G82 L129 D140 MOAD: ic50=0.65nM
PDBbind-CN: -logKd/Ki=9.19,IC50=0.65nM
BindingDB: IC50=0.650000nM,EC50=97nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0000077 DNA damage checkpoint signaling
GO:0006468 protein phosphorylation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hy0, PDBe:2hy0, PDBj:2hy0
PDBsum2hy0
PubMed16990002
UniProtO14757|CHK1_HUMAN Serine/threonine-protein kinase Chk1 (Gene Name=CHEK1)

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