› 5mvh

X-ray diffraction
1.8Å resolution

Glycoside Hydrolase BACCELL_00856

Released:
DOI: 10.2210/pdb5mvh/pdb
PDB entry 5mvh coloured by chain, front view.
PDB entry 5mvh coloured by chain, side view.
PDB entry 5mvh coloured by chain, top view.
Source organism: Bacteroides cellulosilyticus DSM 14838
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-122836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 49.74 KDa
Source organism: Bacteroides cellulosilyticus DSM 14838
Expression system: Escherichia coli
UniProt:
  • Canonical: E2N9B1 (Residues: 23-433; Coverage: 100%)
Gene name: BACCELL_00856
Sequence domains: BNR repeat-containing family member

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 52.842Å b: 68.627Å c: 52.88Å
α: 90° β: 97.72° γ: 90°
R-values:
R R work R free
0.169 0.167 0.214
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