› 3nj3

X-ray diffraction
1.88Å 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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
2 bound ligands:
Ligand ACT 2 x ACT
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P1
Unit cell:
a: 58.338Å b: 58.576Å c: 61.659Å
α: 84.9° β: 70.86° γ: 68.93°
R-values:
R R work R free
0.234 0.231 0.299
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

3 mentions without citation

Domain atrophy creates rare cases of functional partial protein domains.
Prakash et al. (2015)
2 more