› 3wo8

X-ray diffraction
2.43Å resolution

Crystal structure of the beta-N-acetylglucosaminidase from Thermotoga maritima

Released:
DOI: 10.2210/pdb3wo8/pdb
PDB entry 3wo8 coloured by chain, front view.
PDB entry 3wo8 coloured by chain, side view.
PDB entry 3wo8 coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site.
Mine S, Kado Y, Watanabe M, Fukuda Y, Abe Y, Ueda T, Kawarabayasi Y, Inoue T, Ishikawa K
FEBS J 281 5092-103 (2014)
PMID: 25227262

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-N-acetylhexosaminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 53.88 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZR6 (Residues: 1-467; Coverage: 100%)
Gene names: TM_0809, nagA
Sequence domains:
Structure domains: Glycoside hydrolase, family 3, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P3121
Unit cell:
a: 133.457Å b: 133.457Å c: 142.33Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.246
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

On the phosphorylase activity of GH3 enzymes: A β-N-acetylglucosaminidase from Herbaspirillum seropedicae SmR1 and a glucosidase from Saccharopolyspora erythraea.
Ducatti et al. (2016)

1 mention without citation

The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site.
Mine et al. (2014)