PDBe 2bq8

X-ray diffraction
2.2Å resolution

Crystal structure of human purple acid phosphatase with an inhibitory conformation of the repression loop

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tartrate-resistant acid phosphatase type 5 Chain: X
Molecule details ›
Chain: X
Length: 304 amino acids
Theoretical weight: 34.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P13686 (Residues: 22-325; Coverage: 100%)
Gene name: ACP5
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P6122
Unit cell:
a: 94.756Å b: 94.756Å c: 144.007Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.181 0.211
Expression system: Escherichia coli