› 7ov2

X-ray diffraction
2.1Å resolution

Crystal structure of pig purple acid phosphatase in complex with L-glutamine, (poly)ethylene glycol fragments and glycerol

Released:
DOI: 10.2210/pdb7ov2/pdb
PDB entry 7ov2 coloured by chain, front view.
PDB entry 7ov2 coloured by chain, side view.
PDB entry 7ov2 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Rational Design of Potent Inhibitors of a Metallohydrolase Using a Fragment-Based Approach.
Feder D, Mohd-Pahmi SH, Hussein WM, Guddat LW, McGeary RP, Schenk G
ChemMedChem 16 3342-3359 (2021)
PMID: 34331400

Function and Biology Details

Reaction catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Tartrate-resistant acid phosphatase type 5 Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 35.15 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P09889 (Residues: 28-340; Coverage: 98%)
Gene name: ACP5
Sequence domains: Calcineurin-like phosphoesterase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
11 bound ligands:
Ligand 1PE 2 x 1PE
Ligand P6G 1 x P6G
Ligand PG4 2 x PG4
Ligand GLN 28 x GLN
Ligand PO4 1 x PO4
Ligand EDO 17 x EDO
Ligand PGE 8 x PGE
Ligand GOL 13 x GOL
Ligand CIT 1 x CIT
Ligand NA 1 x NA
Ligand FE 2 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 64.447Å b: 68.668Å c: 77.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.142 0.196

Quick links

Citations

1 review citation

The multifaceted nature of plant acid phosphatases: purification, biochemical features, and applications.
Sharma et al. (2023)