› 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:
DOI: 10.2210/pdb1nd5/pdb
PDB entry 1nd5 coloured by chain, front view.
PDB entry 1nd5 coloured by chain, side view.
PDB entry 1nd5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
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.
Ortlund E, LaCount MW, Lebioda L
Biochemistry 42 383-9 (2003)
PMID: 12525165

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer
homo dimer (preferred)
Assembly name:
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
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
4 bound ligands:
Ligand 2BF 4 x 2BF
Ligand 1PE 8 x 1PE
Ligand NDG 1 x NDG
Ligand NAG 1 x NAG
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

Quick links

Citations

6 review citations

The extended human PTPome: a growing tyrosine phosphatase family.
Alonso et al. (2016)
5 more

5 mentions without citation

A combined approach to data mining of textual and structured data to identify cancer-related targets.
Pospisil et al. (2006)
4 more