› 8q1d

X-ray diffraction
1.75Å resolution

D10N variant of beta-phosphoglucomutase from Lactococcus lactis in complex with fructose 1,6-bisphosphate

Released:
DOI: 10.2210/pdb8q1d/pdb
PDB entry 8q1d coloured by chain, front view.
PDB entry 8q1d coloured by chain, side view.
PDB entry 8q1d coloured by chain, top view.
Source organism: Lactococcus lactis subsp. lactis Il1403
Primary publication:
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase.
Cruz-Navarrete FA, Baxter NJ, Flinders AJ, Buzoianu A, Cliff MJ, Baker PJ, Waltho JP
Commun Biol 7 909 (2024)
PMID: 39068257

Function and Biology Details

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

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 Il1403
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

Ligands and Environments

3 bound ligands:
Ligand FBP 1 x FBP
Ligand MG 1 x MG
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 31.888Å b: 71.382Å c: 83.909Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.161 0.252
Expression system: Escherichia coli BL21(DE3)

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