6la0

X-ray diffraction
1.75Å resolution

Crystal structure of AoRut

Released:
Source organism: Aspergillus oryzae
Primary publication:
Aspergillus oryzae Rutinosidase: Biochemical and Structural Investigation.
Appl Environ Microbiol 87 (2021)
PMID: 33218993

Function and Biology Details

Reaction catalysed:
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-103743 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glucan 1,3-beta-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 41.75 KDa
Source organism: Aspergillus oryzae
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1S9DRB1 (Residues: 20-392; Coverage: 100%)
Gene names: Aory04_000396900, OAory_01080470
Sequence domains: Cellulase (glycosyl hydrolase family 5)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 47.908Å b: 169.989Å c: 50.485Å
α: 90° β: 115.619° γ: 90°
R-values:
R R work R free
0.198 0.196 0.23
Expression system: Escherichia coli