› 4kd1

X-ray diffraction
1.7Å resolution

CDK2 in complex with Dinaciclib

Released:
DOI: 10.2210/pdb4kd1/pdb
PDB entry 4kd1 coloured by chain, front view.
PDB entry 4kd1 coloured by chain, side view.
PDB entry 4kd1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cyclin-dependent kinase inhibitor dinaciclib interacts with the acetyl-lysine recognition site of bromodomains.
Martin MP, Olesen SH, Georg GI, Schönbrunn E
ACS Chem Biol 8 2360-5 (2013)
PMID: 24007471

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-dependent kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 33.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P24941 (Residues: 1-298; Coverage: 100%)
Gene names: CDK2, CDKN2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 1 x EDO
Ligand 1QK 1 x 1QK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 53.69Å b: 71.89Å c: 72.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.232
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Targeting bromodomains: epigenetic readers of lysine acetylation.
Filippakopoulos et al. (2014)
28 more

20 mentions without citation

Insights on Structural Characteristics and Ligand Binding Mechanisms of CDK2.
Li et al. (2015)
19 more