› 5if1

X-ray diffraction
2.61Å resolution

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148886 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cyclin-dependent kinase 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 298 amino acids
Theoretical weight: 33.98 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P24941 (Residues: 1-298; Coverage: 100%)
Gene names: CDK2, CDKN2
Sequence domains: Protein kinase domain
Structure domains:
Cyclin-A2 Chains: B, D
Molecule details ›
Chains: B, D
Length: 265 amino acids
Theoretical weight: 30.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20248 (Residues: 174-432; Coverage: 60%)
Gene names: CCN1, CCNA, CCNA2
Sequence domains:
Structure domains: Cyclin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6222
Unit cell:
a: 186.574Å b: 186.574Å c: 213.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.187 0.236
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Kinetics for Drug Discovery: an industry-driven effort to target drug residence time.
Schuetz et al. (2017)
3 more

4 mentions without citation

Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
Kumar et al. (2017)
3 more