4pvi

X-ray diffraction
1.48Å resolution

Crystal structure of GH62 hydrolase in complex with xylotriose

Released:
Source organism: Mycothermus thermophilus
Entry authors: Nocek B, Kaur AP, Xu X, Cui H, Savchenko A

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-100264 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-L-arabinofuranosidase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 38.96 KDa
Source organism: Mycothermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A059U759 (Residues: 30-350; Coverage: 96%)
Gene name: AXH62C
Sequence domains: Glycosyl hydrolase family 62
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P31
Unit cell:
a: 72.445Å b: 72.445Å c: 62.099Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.13 0.129 0.159
Expression system: Escherichia coli