PDBe 4xim

X-ray diffraction
2.3Å resolution

PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 393 amino acids
Theoretical weight: 43.42 KDa
Source organism: Actinoplanes missouriensis
Expression system: Not provided
UniProt:
  • Canonical: P12851 (Residues: 2-394; Coverage: 100%)
Gene names: AMIS_10350, XI, xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 143.45Å b: 143.45Å c: 231.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 not available not available
Expression system: Not provided