› 1hm5

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE RABBIT D-GLUCOSE 6-PHOSPHATE ISOMERASE (NO LIGAND BOUND)

Released:
DOI: 10.2210/pdb1hm5/pdb
PDB entry 1hm5 coloured by chain, front view.
PDB entry 1hm5 coloured by chain, side view.
PDB entry 1hm5 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Conformational changes in phosphoglucose isomerase induced by ligand binding.
Arsenieva D, Jeffery CJ
J Mol Biol 323 77-84 (2002)
PMID: 12368100

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 558 amino acids
Theoretical weight: 62.83 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: Q9N1E2 (Residues: 1-558; Coverage: 100%)
Gene name: GPI
Sequence domains: Phosphoglucose isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 82.756Å b: 115.966Å c: 271.845Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.212

Quick links

Citations

6 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
5 more

3 mentions without citation

Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
Anand et al. (2010)
2 more