3c7g

X-ray diffraction
2.02Å resolution

Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis in complex with xylotetraose.

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-559375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Arabinoxylan arabinofuranohydrolase Chain: A
Molecule details ›
Chain: A
Length: 488 amino acids
Theoretical weight: 51.76 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45071 (Residues: 27-513; Coverage: 100%)
Gene names: BSU18160, xynD
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 67.523Å b: 72.401Å c: 106.869Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.187
Expression system: Escherichia coli