› 2i2w

X-ray diffraction
1.95Å 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 analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-159054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoheptose isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 212 amino acids
Theoretical weight: 23.01 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63224 (Residues: 1-192; Coverage: 100%)
Gene names: JW0212, b0222, gmhA, lpcA, tfrA, yafI
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 83.93Å b: 89.61Å c: 106.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

3 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)
2 more