› 3fm9

X-ray diffraction
2.7Å resolution

Analysis of the Structural Determinants Underlying Discrimination between Substrate and Solvent in beta-Phosphoglucomutase Catalysis

Released:
DOI: 10.2210/pdb3fm9/pdb
PDB entry 3fm9 coloured by chain, front view.
PDB entry 3fm9 coloured by chain, side view.
PDB entry 3fm9 coloured by chain, top view.
Source organism: Lactococcus lactis subsp. lactis
Primary publication:
Analysis of the structural determinants underlying discrimination between substrate and solvent in beta-phosphoglucomutase catalysis.
Dai J, Finci L, Zhang C, Lahiri S, Zhang G, Peisach E, Allen KN, Dunaway-Mariano D
Biochemistry 48 1984-95 (2009)
PMID: 19154134

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 subsp. lactis
Expression system: Escherichia coli
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: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 54.478Å b: 57.656Å c: 77.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.208 0.28
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Enzyme promiscuity: engine of evolutionary innovation.
Pandya et al. (2014)
3 more

1 mention without citation

Analysis of the structural determinants underlying discrimination between substrate and solvent in beta-phosphoglucomutase catalysis.
Dai et al. (2009)