› 6t75

X-ray diffraction
2.55Å resolution

Bacteroides salyersiae GH164 beta-mannosidase 2-deoxy-2-fluoro-beta-D-mannosyl enzyme intermediate

Released:
DOI: 10.2210/pdb6t75/pdb
PDB entry 6t75 coloured by chain, front view.
PDB entry 6t75 coloured by chain, side view.
PDB entry 6t75 coloured by chain, top view.
Source organism: Bacteroides salyersiae
Primary publication:
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164.
Armstrong Z, Davies GJ
OpenAccess logo 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-516259 (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
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

2 bound ligands:
Ligand MAF 6 x MAF
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: 70.155Å b: 104.873Å c: 171.627Å
α: 91.977° β: 97.733° γ: 107.161°
R-values:
R R work R free
0.215 0.214 0.245
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)
4 other articles

1 mention without citation

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