› 1xyn

X-ray diffraction
2Å resolution

STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI

Released:
DOI: 10.2210/pdb1xyn/pdb
PDB entry 1xyn coloured by chain, front view.
PDB entry 1xyn coloured by chain, side view.
PDB entry 1xyn coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei.
Törrönen A, Rouvinen J
Biochemistry 34 847-56 (1995)
PMID: 7827044

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase 1 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 19.05 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: P36218 (Residues: 52-229; Coverage: 85%)
Gene names: M419DRAFT_38418, xyn1
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 72.25Å b: 39.01Å c: 54.3Å
α: 90° β: 91.8° γ: 90°
R-values:
R R work R free
0.185 0.185 not available

Quick links

Citations

6 review citations

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

11 mentions without citation

Molecular structure and catalytic mechanism of fungal family G acidophilic xylanases.
Dey et al. (2018)
10 more