› 5mul

X-ray diffraction
1.39Å resolution

Glycoside Hydrolase BT3686 bound to Glucuronic Acid

Released:
DOI: 10.2210/pdb5mul/pdb
PDB entry 5mul coloured by chain, front view.
PDB entry 5mul coloured by chain, side view.
PDB entry 5mul coloured by chain, top view.
Source organism: Bacteroides thetaiotaomicron VPI-5482
Primary publication:
Unusual active site location and catalytic apparatus in a glycoside hydrolase family.
Munoz-Munoz J, Cartmell A, Terrapon N, Henrissat B, Gilbert HJ
Proc Natl Acad Sci U S A 114 4936-4941 (2017)
PMID: 28396425

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183617 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 49.52 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A1H5 (Residues: 1-1, 21-431; Coverage: 95%)
Gene name: BT_3686
Sequence domains: BNR repeat-containing family member

Ligands and Environments

1 bound ligand:
Ligand BDP 1 x BDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P61
Unit cell:
a: 120.178Å b: 120.178Å c: 52.651Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.194
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.
Bissaro et al. (2018)
4 more

2 mentions without citation

Unusual active site location and catalytic apparatus in a glycoside hydrolase family.
Munoz-Munoz et al. (2017)
1 more