› 2wf5

X-ray diffraction
1.3Å resolution

Structure of Beta-Phosphoglucomutase inhibited with Glucose-6-phosphate and trifluoromagnesate

Released:
DOI: 10.2210/pdb2wf5/pdb
PDB entry 2wf5 coloured by chain, front view.
PDB entry 2wf5 coloured by chain, side view.
PDB entry 2wf5 coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.
Baxter NJ, Bowler MW, Alizadeh T, Cliff MJ, Hounslow AM, Wu B, Berkowitz DB, Williams NH, Blackburn GM, Waltho JP
Proc Natl Acad Sci U S A 107 4555-60 (2010)
PMID: 20164409

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

3 bound ligands:
Ligand BG6 1 x BG6
Ligand MG 2 x MG
Ligand MGF 1 x MGF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 37.647Å b: 54.659Å c: 105.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.192
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Biological phosphoryl-transfer reactions: understanding mechanism and catalysis.
Lassila et al. (2011)
7 more

6 mentions without citation

Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.
Baxter et al. (2010)
5 more