› 2cci

X-ray diffraction
2.7Å resolution

Crystal structure of phospho-CDK2 Cyclin A in complex with a peptide containing both the substrate and recruitment sites of CDC6

Released:
DOI: 10.2210/pdb2cci/pdb
PDB entry 2cci coloured by chain, front view.
PDB entry 2cci coloured by chain, side view.
PDB entry 2cci coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The role of the phospho-CDK2/cyclin A recruitment site in substrate recognition.
Cheng KY, Noble ME, Skamnaki V, Brown NR, Lowe ED, Kontogiannis L, Shen K, Cole PA, Siligardi G, Johnson LN
J Biol Chem 281 23167-79 (2006)
PMID: 16707497

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

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148906 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cyclin-dependent kinase 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 299 amino acids
Theoretical weight: 34.14 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:
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
Cell division control protein 6 homolog Chains: F, I
Molecule details ›
Chains: F, I
Length: 30 amino acids
Theoretical weight: 3.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q99741 (Residues: 71-100; Coverage: 5%)
Gene names: CDC18L, CDC6

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 74.42Å b: 114.389Å c: 170.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.261 0.321
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

17 review citations

Mechanisms of specificity in protein phosphorylation.
Ubersax et al. (2007)
16 more

16 mentions without citation

Physicochemical mechanisms of protein regulation by phosphorylation.
Nishi et al. (2014)
15 more