› 6k5j

X-ray diffraction
1.9Å resolution

Structure of a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7

Released:
DOI: 10.2210/pdb6k5j/pdb
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Source organism: Paenibacillaceae
Primary publication:
Structural and functional characterization of a glycoside hydrolase family 3 β-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7.
Itoh T, Araki T, Nishiyama T, Hibi T, Kimoto H
J Biochem 166 503-515 (2019)
PMID: 31501879

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-288674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 3 N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 535 amino acids
Theoretical weight: 57.05 KDa
Source organism: Paenibacillaceae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A5S8WF56 (Residues: 1-535; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 3 N terminal domain

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand GOL 1 x GOL
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P43212
Unit cell:
a: 84.23Å b: 84.23Å c: 157.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.204
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

Structural characterization of two solute-binding proteins for N,N'-diacetylchitobiose/N,N',N''-triacetylchitotoriose of the gram-positive bacterium, Paenibacillus sp. str. FPU-7.
Itoh et al. (2021)

2 mentions without citation

Chitinolytic Enzymes of the Hyperparasite Fungus Aphanocladium album: Genome-Wide Survey and Characterization of A Selected Enzyme.
Leoni et al. (2023)
1 more

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