1nd5

X-ray diffraction
2.9Å resolution

Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design

Released:

Function and Biology Details

Reactions catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate

Structure analysis Details

Assemblies composition:
homo trimer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-147308 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Prostatic acid phosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 354 amino acids
Theoretical weight: 41.05 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P15309 (Residues: 33-386; Coverage: 100%)
Gene names: ACP3, ACPP
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 120.1Å b: 204.86Å c: 71.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.279