› 2wfa

X-ray diffraction
1.65Å resolution

Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.

Released:
DOI: 10.2210/pdb2wfa/pdb
PDB entry 2wfa coloured by chain, front view.
PDB entry 2wfa coloured by chain, side view.
PDB entry 2wfa coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.
Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP
Proc Natl Acad Sci U S A 109 6910-5 (2012)
PMID: 22505741

Function and Biology Details

Reaction catalysed: 
Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-phosphoglucomutase Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.24 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P71447 (Residues: 1-221; Coverage: 100%)
Gene names: L0001, LL0429, pgmB
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand BEF 1 x BEF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 53.3Å b: 57.3Å c: 75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes.
Jin et al. (2017)
3 more

5 mentions without citation

Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.
Griffin et al. (2012)
4 more