› 1z4o

X-ray diffraction
1.9Å resolution

Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate

Released:
DOI: 10.2210/pdb1z4o/pdb
PDB entry 1z4o coloured by chain, front view.
PDB entry 1z4o coloured by chain, side view.
PDB entry 1z4o coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
Chemical confirmation of a pentavalent phosphorane in complex with beta-phosphoglucomutase.
Tremblay LW, Zhang G, Dai J, Dunaway-Mariano D, Allen KN
J Am Chem Soc 127 5298-9 (2005)
PMID: 15826149

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 domain:

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 24.24 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli BL21(DE3)
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 2 x MG
Ligand GL1 2 x GL1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 55.069Å b: 36.351Å c: 104.883Å
α: 90° β: 101.77° γ: 90°
R-values:
R R work R free
0.205 0.199 0.254
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes.
Schramm VL. (2011)
1 more

1 mention without citation

An Enzyme with High Catalytic Proficiency Utilizes Distal Site Substrate Binding Energy to Stabilize the Closed State but at the Expense of Substrate Inhibition.
Robertson et al. (2022)