3nbu

X-ray diffraction
2.05Å resolution

Crystal structure of pGI glucosephosphate isomerase

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate isomerase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 549 amino acids
Theoretical weight: 61.63 KDa
Source organism: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P0A6T1 (Residues: 1-549; Coverage: 100%)
Gene names: JW3985, b4025, pgi
Sequence domains: Phosphoglucose isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P1
Unit cell:
a: 69.806Å b: 72.874Å c: 181.851Å
α: 92.47° β: 97.82° γ: 114.57°
R-values:
R R work R free
0.172 0.169 0.23