› 3o5s

X-ray diffraction
2.2Å resolution

Crystal Structure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168)

Released:
DOI: 10.2210/pdb3o5s/pdb
PDB entry 3o5s coloured by chain, front view.
PDB entry 3o5s coloured by chain, side view.
PDB entry 3o5s coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Biochemical and structural characterization of a Beta-1,3 1,4-glucanase from Bacillus subtilis 168
Furtado GP, Ribeiro LF, Santos CR, Tonoli CC, De Souza AR, Oliveira RR, Tyago M
PROCESS BIOCHEM 46 1202-1206 (2011)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucanase Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 26.87 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P04957 (Residues: 29-242; Coverage: 100%)
Gene names: BSU39070, N15B, bgl, bglS, licS
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand B3P 1 x B3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P43212
Unit cell:
a: 103.758Å b: 103.758Å c: 102.097Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.249 0.292
Expression system: Escherichia coli

Quick links