› 5mqr

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H(2)O = 4-O-(beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183763 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Six-hairpin glycosidase Chain: A
Molecule details ›
Chain: A
Length: 1108 amino acids
Theoretical weight: 129.22 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A8Z7 (Residues: 21-1109; Coverage: 100%)
Gene name: BT_1020
Sequence domains:

Ligands and Environments

5 bound ligands:
Ligand CA 2 x CA
Ligand PGE 2 x PGE
Ligand EPE 2 x EPE
Ligand EDO 2 x EDO
Ligand NA 1 x NA
2 modified residues:
Ligand MSE 36 x MSE
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 125.72Å b: 316.998Å c: 90.023Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.195
Expression system: Escherichia coli

Quick links

Citations

45 review citations

Interactions of commensal and pathogenic microorganisms with the intestinal mucosal barrier.
Martens et al. (2018)
44 more

1 mention without citation

Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121.
Saito et al. (2020)