PDBe 1tux

X-ray diffraction
1.8Å resolution

HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE XYLANASE FROM THERMOASCUS AURANTIACUS

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. 
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 301 amino acids
Theoretical weight: 32.56 KDa
Source organism: Thermoascus aurantiacus
UniProt:
  • Canonical: P23360 (Residues: 28-327; Coverage: 99%)
Gene name: XYNA
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 41.69Å b: 68.1Å c: 51.44Å
α: 90° β: 113.59° γ: 90°
R-values:
R R work R free
0.16 0.16 0.211