› 1pcj

X-ray diffraction
2Å resolution

Enzyme-ligand complex of P. aeruginosa PMM/PGM

Released:
DOI: 10.2210/pdb1pcj/pdb
PDB entry 1pcj coloured by chain, front view.
PDB entry 1pcj coloured by chain, side view.
PDB entry 1pcj coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
Regni C, Naught L, Tipton PA, Beamer LJ
Structure 12 55-63 (2004)
PMID: 14725765

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: 50.43 KDa
Source organism: Pseudomonas aeruginosa
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 M1P 1 x M1P
Ligand ZN 1 x ZN
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 70.896Å b: 74.307Å c: 85.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.163 0.203
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Understanding the control of Pseudomonas aeruginosa alginate synthesis and the prospects for management of chronic infections in cystic fibrosis.
Ramsey et al. (2005)
3 more

4 mentions without citation

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