› 2fkm

X-ray diffraction
1.9Å resolution

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

Released:
DOI: 10.2210/pdb2fkm/pdb
PDB entry 2fkm coloured by chain, front view.
PDB entry 2fkm coloured by chain, side view.
PDB entry 2fkm coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.
Regni C, Schramm AM, Beamer LJ
J Biol Chem 281 15564-71 (2006)
PMID: 16595672

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 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: X
Molecule details ›
Chain: X
Length: 462 amino acids
Theoretical weight: 50.25 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26276 (Residues: 2-463; Coverage: 100%)
Gene names: PA5322, algC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand G16 1 x G16
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P212121
Unit cell:
a: 70.222Å b: 70.356Å c: 84.392Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

4 mentions without citation

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