› 1dyo

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Y Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.86 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli
UniProt:
  • Canonical: P51584 (Residues: 558-718; Coverage: 15%)
Gene name: xynY
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6122
Unit cell:
a: 89.49Å b: 89.49Å c: 207.69Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.25
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates.
Fontes et al. (2010)
5 more

12 mentions without citation

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
11 more