Structure of PDB 2brg Chain A

Receptor sequence
>2brgA (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
EDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKENIKKEICINKML
NHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFH
QLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRER
LLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPS
DSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKD
RWYNKPL
3D structure
PDB2brg Structure-Based Design of Novel Chk1 Inhibitors: Insights Into Hydrogen Bonding and Protein-Ligand Affinity.
ChainA
Resolution2.1 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 DFY A L15 G16 A36 E85 Y86 C87 G90 E91 L9 G10 A30 E73 Y74 C75 G78 E79 MOAD: ic50=6.1uM
PDBbind-CN: -logKd/Ki=5.21,IC50=6.1uM
BindingDB: IC50=6100nM
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:2brg, PDBe:2brg, PDBj:2brg
PDBsum2brg
PubMed15974586
UniProtO14757|CHK1_HUMAN Serine/threonine-protein kinase Chk1 (Gene Name=CHEK1)

[Back to BioLiP]