4xut

X-ray diffraction
1.8Å resolution

Structure of the CBM22-2 xylan-binding domain in complex with 1,3:1,4 Beta-glucotetraose B from Paenibacillus barcinonensis Xyn10C

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-xylanase C Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 181 amino acids
Theoretical weight: 19.92 KDa
Source organism: Paenibacillus barcinonensis
Expression system: Escherichia coli
UniProt:
  • Canonical: O69230 (Residues: 186-366; Coverage: 17%)
Gene name: xynC
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P32
Unit cell:
a: 92.478Å b: 92.478Å c: 48.382Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.204 0.226
Expression system: Escherichia coli