› 3moz

X-ray diffraction
1.6Å resolution

Structure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol (1,2,3,5,6)pentakisphosphate

Released:
DOI: 10.2210/pdb3moz/pdb
PDB entry 3moz coloured by chain, front view.
PDB entry 3moz coloured by chain, side view.
PDB entry 3moz coloured by chain, top view.
Source organism: Selenomonas ruminantium
Primary publication:
Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.
Gruninger RJ, Dobing S, Smith AD, Bruder LM, Selinger LB, Wieden HJ, Mosimann SC
J Biol Chem 287 9722-9730 (2012)
PMID: 22139834

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine specific protein phosphatases domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 36.16 KDa
Source organism: Selenomonas ruminantium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7WUJ1 (Residues: 33-346; Coverage: 98%)
Gene name: phyA
Sequence domains: Inositol hexakisphosphate
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand PO4 2 x PO4
Ligand 5IP 2 x 5IP
Ligand GOL 8 x GOL
Ligand ACT 4 x ACT
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 46Å b: 137.21Å c: 79.99Å
α: 90° β: 102.97° γ: 90°
R-values:
R R work R free
0.168 0.164 0.184
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance.
Juers et al. (2012)
5 other articles

1 mention without citation

Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.
Gruninger et al. (2012)