2hpa

X-ray diffraction
2.9Å resolution

STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE

Released:
Source organism: Homo sapiens

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 dimer
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-147310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
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 names: ACP3, ACPP
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 119.86Å b: 202.68Å c: 71.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.308