› 1e59

X-ray diffraction
1.3Å resolution

E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate

Released:
DOI: 10.2210/pdb1e59/pdb
PDB entry 1e59 coloured by chain, front view.
PDB entry 1e59 coloured by chain, side view.
PDB entry 1e59 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex.
Bond CS, White MF, Hunter WN
J Mol Biol 316 1071-81 (2002)
PMID: 11884145

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158665 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 28.47 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62707 (Residues: 2-250; Coverage: 100%)
Gene names: JW0738, b0755, gpm, gpmA, pgm, pgmA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

2 bound ligands:
Ligand VO3 1 x VO3
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21212
Unit cell:
a: 61.249Å b: 112.142Å c: 40.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 not available 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
2 more

11 mentions without citation

The use of polyoxometalates in protein crystallography - An attempt to widen a well-known bottleneck.
Bijelic et al. (2015)
10 more