› 6t7g

X-ray diffraction
1.8Å resolution

Bacteroides salyersiae GH164 beta-mannosidase in complex with mannoimidazole

Released:
DOI: 10.2210/pdb6t7g/pdb
PDB entry 6t7g coloured by chain, front view.
PDB entry 6t7g coloured by chain, side view.
PDB entry 6t7g coloured by chain, top view.
Source organism: Bacteroides salyersiae CL02T12C01
Primary publication:
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164.
Armstrong Z, Davies GJ
J Biol Chem 295 4316-4326 (2020)
PMID: 31871050

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase trimerisation domain-containing protein Chains: AAA, BBB, CCC, DDD, EEE, FFF
Molecule details ›
Chains: AAA, BBB, CCC, DDD, EEE, FFF
Length: 674 amino acids
Theoretical weight: 76.68 KDa
Source organism: Bacteroides salyersiae CL02T12C01
Expression system: Escherichia coli
UniProt:
  • Canonical: I9SUA3 (Residues: 22-673; Coverage: 97%)
Gene name: HMPREF1071_03408
Sequence domains: Beta-galactosidase trimerisation domain

Ligands and Environments

3 bound ligands:
Ligand EDO 16 x EDO
Ligand MVL 6 x MVL
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P1
Unit cell:
a: 69.71Å b: 104.743Å c: 170.568Å
α: 92.29° β: 97.273° γ: 106.301°
R-values:
R R work R free
0.208 0.206 0.231
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Towards an understanding of the enzymatic degradation of complex plant mannan structures.
Mafa et al. (2023)
3 other articles

2 mentions without citation

Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164.
Armstrong et al. (2020)
1 more