› 3niy

X-ray diffraction
1.58Å 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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107634 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 341 amino acids
Theoretical weight: 40.42 KDa
Source organism: Thermotoga petrophila RKU-1
Expression system: Escherichia coli
UniProt:
  • Canonical: A5IL00 (Residues: 21-344; Coverage: 93%)
Gene name: Tpet_0854
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand ACT 5 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P1
Unit cell:
a: 58.538Å b: 58.554Å c: 61.579Å
α: 84.54° β: 70.82° γ: 68.87°
R-values:
R R work R free
0.16 0.158 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Classification, mode of action and production strategy of xylanase and its application for biofuel production from water hyacinth.
Uday et al. (2016)
1 more

5 mentions without citation

High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.
Hassan et al. (2013)
4 more