PDBe 1cvi

X-ray diffraction
3.2Å resolution

CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human prostatic acid phosphatase .
Prostate 42 211-8 (2000)
PMID: 10639192

Function and Biology Details

Reactions catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostatic acid phosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 342 amino acids
Theoretical weight: 39.78 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P15309 (Residues: 33-374; Coverage: 97%)
Gene name: ACPP
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 126.33Å b: 207.96Å c: 73.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 0.274