PDBe 1fq1

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2

Released:

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein. 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cyclin-dependent kinase 2 Chain: B
Molecule details ›
Chain: B
Length: 298 amino acids
Theoretical weight: 34.06 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-dependent kinase inhibitor 3 Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16667 (Residues: 1-212; Coverage: 100%)
Gene names: CDI1, CDKN3, CIP2, KAP
Sequence domains: Cyclin-dependent kinase inhibitor 3 (CDKN3)
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3221
Unit cell:
a: 134.45Å b: 134.45Å c: 65.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.235 0.313
Expression system: Escherichia coli