› 3qu2

X-ray diffraction
1.95Å resolution

Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, a closed cap conformation

Released:
DOI: 10.2210/pdb3qu2/pdb
PDB entry 3qu2 coloured by chain, front view.
PDB entry 3qu2 coloured by chain, side view.
PDB entry 3qu2 coloured by chain, top view.
Source organism: Bacteroides thetaiotaomicron
Primary publication:
Divergence of structure and function in the haloacid dehalogenase enzyme superfamily: Bacteroides thetaiotaomicron BT2127 is an inorganic pyrophosphatase.
Huang H, Patskovsky Y, Toro R, Farelli JD, Pandya C, Almo SC, Allen KN, Dunaway-Mariano D
Biochemistry 50 8937-49 (2011)
PMID: 21894910

Function and Biology Details

Reaction catalysed: 
Diphosphate + H(2)O = 2 phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
homo trimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-183705 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-phosphoglucomutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 243 amino acids
Theoretical weight: 27.01 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Not provided
UniProt:
  • Canonical: Q8A5V9 (Residues: 1-224; Coverage: 100%)
Gene name: BT_2127
Sequence domains: Haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 4 x MG
Ligand GOL 8 x GOL
Ligand CIT 1 x CIT
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 137.602Å b: 71.761Å c: 114.525Å
α: 90° β: 105.8° γ: 90°
R-values:
R R work R free
0.234 0.232 0.275
Expression system: Not provided

Quick links

Citations

4 review citations

Enzyme promiscuity: engine of evolutionary innovation.
Pandya et al. (2014)
3 more

3 mentions without citation

Catalytic scaffolds for phosphoryl group transfer.
Allen et al. (2016)
2 more