› 3bkq

X-ray diffraction
2.05Å resolution

Structure of the P368G mutant of PMM/PGM in complex with its substrate

Released:
DOI: 10.2210/pdb3bkq/pdb
PDB entry 3bkq coloured by chain, front view.
PDB entry 3bkq coloured by chain, side view.
PDB entry 3bkq coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa.
Schramm AM, Mehra-Chaudhary R, Furdui CM, Beamer LJ
Biochemistry 47 9154-62 (2008)
PMID: 18690721

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: 463 amino acids
Theoretical weight: 50.39 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26276 (Residues: 1-463; Coverage: 100%)
Gene names: PA5322, algC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand G1P 1 x G1P
Ligand ZN 1 x ZN
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: 70.604Å b: 74.74Å c: 86.924Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.249
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

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

2 mentions without citation

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