› 1pvx

X-ray diffraction
1.59Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 20.96 KDa
Source organism: Paecilomyces variotii
UniProt:
  • Canonical: P81536 (Residues: 1-194; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 38.762Å b: 54.058Å c: 90.064Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.219

Quick links

Citations

5 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
4 more

3 mentions without citation

Structural analysis of a glycoside hydrolase family 11 xylanase from Neocallimastix patriciarum: insights into the molecular basis of a thermophilic enzyme.
Cheng et al. (2014)
2 more