› 1ihp

X-ray diffraction
2.5Å resolution

STRUCTURE OF PHOSPHOMONOESTERASE

Released:
DOI: 10.2210/pdb1ihp/pdb
PDB entry 1ihp coloured by chain, front view.
PDB entry 1ihp coloured by chain, side view.
PDB entry 1ihp coloured by chain, top view.
Source organism: Aspergillus ficuum
Primary publication:
Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.
Kostrewa D, Grüninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP
Nat Struct Biol 4 185-90 (1997)
PMID: 9164457

Function and Biology Details

Reaction catalysed: 
Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-152723 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phytase A Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 48.24 KDa
Source organism: Aspergillus ficuum
UniProt:
  • Canonical: P34752 (Residues: 30-467; Coverage: 99%)
Gene name: phyA
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P321
Unit cell:
a: 92.25Å b: 92.25Å c: 100.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.155 0.211

Quick links

Citations

13 review citations

Phytases: microbial sources, production, purification, and potential biotechnological applications.
Vohra et al. (2003)
12 more

4 mentions without citation

Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.
Cho et al. (2008)
3 more