› 3akg

X-ray diffraction
1.8Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 51.94 KDa
Source organism: Streptomyces avermitilis MA-4680 = NBRC 14893
Expression system: Escherichia coli
UniProt:
  • Canonical: Q82P90 (Residues: 28-481; Coverage: 100%)
Gene names: Araf43A, SAVERM_1043, abfA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: AHR
Carbohydrate polymer
4 bound ligands:
Ligand CL 1 x CL
Ligand NA 1 x NA
Ligand AHR 2 x AHR
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 41.052Å b: 91.765Å c: 135.053Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.221
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Specific and non-specific enzymes for furanosyl-containing conjugates: biosynthesis, metabolism, and chemo-enzymatic synthesis.
Chlubnova et al. (2012)
3 more

1 mention without citation

Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43.
Fujimoto et al. (2010)