1fpz

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-172552 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-dependent kinase inhibitor 3 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P65
Unit cell:
a: 131.93Å b: 131.93Å c: 140.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.253
Expression system: Escherichia coli