X-ray diffraction
1.8Å resolution

Crystal Structure of a GH8 catalytic mutant xylohexaose complex xylanase from Teredinibacter turnerae


Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Cellulase Chain: A
Molecule details ›
Chain: A
Length: 399 amino acids
Theoretical weight: 45.11 KDa
Source organism: Teredinibacter turnerae T7901
Expression system: Escherichia coli
  • Canonical: C5BJ89 (Residues: 41-436; Coverage: 97%)
Gene name: TERTU_4506
Sequence domains: Glycosyl hydrolases family 8
Structure domains: Glycosyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 60.973Å b: 79.694Å c: 88.01Å
α: 90° β: 90° γ: 90°
R R work R free
0.17 0.169 0.199
Expression system: Escherichia coli