› 1goo

X-ray diffraction
1.87Å resolution

Thermostable xylanase I from Thermoascus aurantiacus - Cryocooled glycerol complex

Released:
DOI: 10.2210/pdb1goo/pdb
PDB entry 1goo coloured by chain, front view.
PDB entry 1goo coloured by chain, side view.
PDB entry 1goo coloured by chain, top view.
Source organism: Thermoascus aurantiacus
Primary publication:
Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A.
Lo Leggio L, Kalogiannis S, Eckert K, Teixeira SC, Bhat MK, Andrei C, Pickersgill RW, Larsen S
FEBS Lett 509 303-8 (2001)
PMID: 11741607

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-149932 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 32.89 KDa
Source organism: Thermoascus aurantiacus
UniProt:
  • Canonical: P23360 (Residues: 27-329; Coverage: 100%)
Gene name: XYNA
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 45.61Å b: 58.947Å c: 50.752Å
α: 90° β: 111.67° γ: 90°
R-values:
R R work R free
0.175 0.175 0.207

Quick links

Citations

3 review citations

Computational enzyme design.
Kiss et al. (2013)
2 more

1 mention without citation

Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity.
Korman et al. (2004)