3gw8

X-ray diffraction
1.93Å resolution

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with vanadate and glycerol

Released:

Function and Biology Details

Reaction catalysed:
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-174691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 28.96 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JWH7 (Residues: 1-249; Coverage: 100%)
Gene names: BURPS1710b_0662, gpmA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 45.175Å b: 49.112Å c: 62.59Å
α: 106.42° β: 91.18° γ: 107.61°
R-values:
R R work R free
0.189 0.187 0.227
Expression system: Escherichia coli