› 1ol1

X-ray diffraction
2.9Å resolution

Cyclin A binding groove inhibitor H-Cit-Cit-Leu-Ile-(p-F-Phe)-NH2

Released:
DOI: 10.2210/pdb1ol1/pdb
PDB entry 1ol1 coloured by chain, front view.
PDB entry 1ol1 coloured by chain, side view.
PDB entry 1ol1 coloured by chain, top view.
Source organisms:
Primary publication:
Insights into cyclin groove recognition: complex crystal structures and inhibitor design through ligand exchange.
Kontopidis G, Andrews MJ, McInnes C, Cowan A, Powers H, Innes L, Plater A, Griffiths G, Paterson D, Zheleva DI, Lane DP, Green S, Walkinshaw MD, Fischer PM
Structure 11 1537-46 (2003)
PMID: 14656438

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-148893 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 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: 260 amino acids
Theoretical weight: 29.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20248 (Residues: 173-432; Coverage: 60%)
Gene names: CCN1, CCNA, CCNA2
Sequence domains:
Structure domains: Cyclin-like
CIR-CIR-LEU-ILE-PFF-NH2 Chains: F, H
Molecule details ›
Chains: F, H
Length: 6 amino acids
Theoretical weight: 722 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand CIR 4 x CIR
Ligand PFF 2 x PFF

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 74.498Å b: 113.471Å c: 154.482Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.284
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Protein kinase inhibitors: contributions from structure to clinical compounds.
Johnson LN. (2009)
3 more

1 mention without citation

GEMMI and Servalcat restrain REFMAC5.
Yamashita et al. (2023)