3ezn

X-ray diffraction
2.1Å resolution

Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b

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

Assemblies composition:
monomeric (preferred)
homo dimer
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 1710b
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 44.94Å b: 49.08Å c: 62.11Å
α: 107.11° β: 91.19° γ: 107.81°
R-values:
R R work R free
0.152 0.15 0.204
Expression system: Escherichia coli