› 1jst

X-ray diffraction
2.6Å resolution

PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A

Released:
DOI: 10.2210/pdb1jst/pdb
PDB 1jst coloured by chain and viewed from the front.
PDB 1jst coloured by chain and viewed from the side.
PDB 1jst coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural basis of cyclin-dependent kinase activation by phosphorylation.
Russo AA, Jeffrey PD, Pavletich NP
Nat. Struct. Biol. 3 696-700 (1996)
PMID: 8756328

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (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: 34.06 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: 258 amino acids
Theoretical weight: 29.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20248 (Residues: 175-432; Coverage: 60%)
Gene names: CCN1, CCNA, CCNA2
Sequence domains:
Structure domains: Cyclin-like

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand ATP 2 x ATP
1 modified residue:
Ligand TPO 2 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 139.6Å b: 149.1Å c: 74.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 not available
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli

Quick links

Citations

82 review citations

Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.
Seok SH. (2021)
81 more

23 mentions without citation

Structural insights into the functional diversity of the CDK-cyclin family.
Wood et al. (2018)
22 more