› 5la1

X-ray diffraction
1.9Å resolution

The mechanism by which arabinoxylanases can recognise highly decorated xylans

Released:
DOI: 10.2210/pdb5la1/pdb
PDB entry 5la1 coloured by chain, front view.
PDB entry 5la1 coloured by chain, side view.
PDB entry 5la1 coloured by chain, top view.
Source organism: Acetivibrio thermocellus JW20
Primary publication:
The Mechanism by Which Arabinoxylanases Can Recognize Highly Decorated Xylans.
Labourel A, Crouch LI, Brás JL, Jackson A, Rogowski A, Gray J, Yadav MP, Henrissat B, Fontes CM, Gilbert HJ, Najmudin S, Baslé A, Cuskin F
J Biol Chem 291 22149-22159 (2016)
PMID: 27531750

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107066 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbohydrate binding family 6 Chain: A
Molecule details ›
Chain: A
Length: 491 amino acids
Theoretical weight: 54.16 KDa
Source organism: Acetivibrio thermocellus JW20
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DHG6 (Residues: 37-516; Coverage: 51%)
Gene name: Cthe_2193
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand XYP 2 x XYP
Ligand CA 3 x CA
Ligand 144 3 x 144
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P212121
Unit cell:
a: 67.911Å b: 72.514Å c: 109.537Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.131 0.129 0.16
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.
Nordberg Karlsson et al. (2018)
1 more

2 mentions without citation

Enhanced oxide ion conductivity in stabilized delta-Bi2O3.
Punn et al. (2006)
1 more