› 4mgq

X-ray diffraction
1.68Å resolution

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 18.75 KDa
Source organism: Prevotella bryantii B14
Expression system: Escherichia coli
UniProt:
  • Canonical: D8DVU6 (Residues: 136-303; Coverage: 30%)
Gene name: PBR_0377
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P3121
Unit cell:
a: 68.683Å b: 68.683Å c: 111.471Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.182 0.209
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Polysaccharide Utilization Loci: Fueling Microbial Communities.
Grondin et al. (2017)
14 more

2 mentions without citation

Xylan utilization in human gut commensal bacteria is orchestrated by unique modular organization of polysaccharide-degrading enzymes.
Zhang et al. (2014)
1 more