Structure of PDB 2qhn Chain A

Receptor sequence
>2qhnA (length=268) Species: 9606 (Homo sapiens) [Search protein sequence]
AVPFVEDWDLVQTLGGEVQLAVNRVTEEAVAVKIVDMKNIKKEICINKML
NHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFH
QLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRER
LLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPS
DSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKD
RWYNKPLKKGAKRPRVTS
3D structure
PDB2qhn Optimization of a pyrazoloquinolinone class of Chk1 kinase inhibitors.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D130 K132 E134 N135 D148 T170
Catalytic site (residue number reindexed from 1) D118 K120 E122 N123 D136 T158
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 582 A L15 G16 A36 E85 Y86 C87 G90 L137 L14 G15 A31 E73 Y74 C75 G78 L125 MOAD: ic50=980nM
PDBbind-CN: -logKd/Ki=6.01,IC50=980nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qhn, PDBe:2qhn, PDBj:2qhn
PDBsum2qhn
PubMed17804227
UniProtO14757|CHK1_HUMAN Serine/threonine-protein kinase Chk1 (Gene Name=CHEK1)

[Back to BioLiP]