› 4mrq

X-ray diffraction
1.9Å resolution

Crystal Structure of wild-type unphosphorylated PMM/PGM

Released:
DOI: 10.2210/pdb4mrq/pdb
PDB entry 4mrq coloured by chain, front view.
PDB entry 4mrq coloured by chain, side view.
PDB entry 4mrq coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase.
Lee Y, Villar MT, Artigues A, Beamer LJ
J Biol Chem 289 4674-82 (2014)
PMID: 24403075

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: 455 amino acids
Theoretical weight: 49.56 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26276 (Residues: 9-463; Coverage: 98%)
Gene names: PA5322, algC
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand TLA 1 x TLA
Ligand EDO 4 x EDO
Ligand PEG 5 x PEG
Ligand PGE 3 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 70.541Å b: 72.003Å c: 92.349Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.205
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Applications of hydrogen/deuterium exchange MS from 2012 to 2014.
Pirrone et al. (2015)
1 more

3 mentions without citation

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