› 4il8

X-ray diffraction
1.8Å resolution

Crystal structure of an H329A mutant of p. aeruginosa PMM/PGM

Released:
DOI: 10.2210/pdb4il8/pdb
PDB entry 4il8 coloured by chain, front view.
PDB entry 4il8 coloured by chain, side view.
PDB entry 4il8 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Identification of an essential active-site residue in the α-D-phosphohexomutase enzyme superfamily.
Lee Y, Mehra-Chaudhary R, Furdui C, Beamer LJ
FEBS J 280 2622-32 (2013)
PMID: 23517223

Function and Biology Details

Reactions catalysed: 
Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150685 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphomannomutase/phosphoglucomutase Chain: A
Molecule details ›
Chain: A
Length: 463 amino acids
Theoretical weight: 50.39 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P26276 (Residues: 1-463; Coverage: 100%)
Gene names: PA5322, algC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GOL 2 x GOL
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 70.962Å b: 72.906Å c: 93.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mutations in hereditary phosphoglucomutase 1 deficiency map to key regions of enzyme structure and function.
Beamer LJ. (2015)
9 other articles

2 mentions without citation

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.
Stiers et al. (2017)
1 more