› 6ydk

X-ray diffraction
2.02Å resolution

Substrate-free P146A variant of beta-phosphoglucomutase from Lactococcus lactis

Released:
DOI: 10.2210/pdb6ydk/pdb
PDB entry 6ydk coloured by chain, front view.
PDB entry 6ydk coloured by chain, side view.
PDB entry 6ydk coloured by chain, top view.
Source organism: Lactococcus lactis subsp. lactis Il1403
Primary publication:
Allomorphy as a mechanism of post-translational control of enzyme activity.
Wood HP, Cruz-Navarrete FA, Baxter NJ, Trevitt CR, Robertson AJ, Dix SR, Hounslow AM, Cliff MJ, Waltho JP
OpenAccess logo Nat Commun 11 5538 (2020)
PMID: 33139716

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: 24.21 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 53.3Å b: 56.24Å c: 77.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

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)

1 mention without citation

Allomorphy as a mechanism of post-translational control of enzyme activity.
Wood et al. (2020)