PDBe 1xih

X-ray diffraction
1.7Å resolution

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

Released:
Source organism: Streptomyces rubiginosus
Primary publication:
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase.
Acta Crystallogr. D Biol. Crystallogr. 50 113-23 (1994)
PMID: 15299449

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: 388 amino acids
Theoretical weight: 43.25 KDa
Source organism: Streptomyces rubiginosus
Expression system: Not provided
UniProt:
  • Canonical: P24300 (Residues: 1-388; Coverage: 100%)
Gene name: xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 93.66Å b: 100.02Å c: 102.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 not available not available
Expression system: Not provided