› 3bjz

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reaction catalysed: 
D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoheptose isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 199 amino acids
Theoretical weight: 21.86 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HVZ0 (Residues: 1-197; Coverage: 100%)
Gene names: PA4425, gmhA
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 123.842Å b: 131.609Å c: 48.774Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.197 0.274
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The return of metabolism: biochemistry and physiology of the pentose phosphate pathway.
Stincone et al. (2015)
3 more

4 mentions without citation

Functional and structural studies on the Neisseria gonorrhoeae GmhA, the first enzyme in the glycero-manno-heptose biosynthesis pathways, demonstrate a critical role in lipooligosaccharide synthesis and gonococcal viability.
Wierzbicki et al. (2017)
3 more