5o80

X-ray diffraction
2.92Å resolution

Crystal Structure of R67A Mutant of alpha-L-arabinofuranosidase Ara51 from Clostridium thermocellum in complex with L-Arabinofuranose

Released:
Source organism: Chaetomium thermophilum
Entry authors: Lafite P, Daniellou R

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:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 501 amino acids
Theoretical weight: 57.43 KDa
Source organism: Chaetomium thermophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DIH0 (Residues: 2-502; Coverage: 100%)
Gene name: Cthe_2548
Sequence domains: Alpha-L-arabinofuranosidase C-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43212
Unit cell:
a: 173.74Å b: 173.74Å c: 271.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.246
Expression system: Escherichia coli