› 2whe

X-ray diffraction
1.55Å resolution

Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands.

Released:
DOI: 10.2210/pdb2whe/pdb
PDB entry 2whe coloured by chain, front view.
PDB entry 2whe coloured by chain, side view.
PDB entry 2whe 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

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 53.239Å b: 56.9Å c: 75.441Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.208
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

5 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)
4 more