› 2fkf

X-ray diffraction
2Å resolution

Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound

Released:
DOI: 10.2210/pdb2fkf/pdb
Model geometry
Fit model/data
PDB entry 2fkf coloured by chain, front view.
PDB entry 2fkf coloured by chain, side view.
PDB entry 2fkf 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: A
Molecule details ›
Chain: A
Length: 462 amino acids
Theoretical weight: 50.3 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
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 70.865Å b: 72.849Å c: 91.258Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.24
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