PDBe 3xis

X-ray diffraction
1.6Å resolution

A METAL-MEDIATED HYDRIDE SHIFT MECHANISM FOR XYLOSE ISOMERASE BASED ON THE 1.6 ANGSTROMS STREPTOMYCES RUBIGINOSUS STRUCTURES WITH XYLITOL AND D-XYLOSE

Released:

Function and Biology Details

Reaction catalysed:
D-xylopyranose = D-xylulose. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylose isomerase Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 43.15 KDa
Source organism: Streptomyces rubiginosus
Expression system: Not provided
UniProt:
  • Canonical: P24300 (Residues: 2-388; Coverage: 100%)
Gene name: xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 94.64Å b: 99.97Å c: 103.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 not available not available
Expression system: Not provided