› 1mac

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE

Released:
DOI: 10.2210/pdb1mac/pdb
PDB entry 1mac coloured by chain, front view.
PDB entry 1mac coloured by chain, side view.
PDB entry 1mac coloured by chain, top view.
Source organism: Paenibacillus macerans
Primary publication:
Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase.
Hahn M, Olsen O, Politz O, Borriss R, Heinemann U
J Biol Chem 270 3081-8 (1995)
PMID: 7852389

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 23.83 KDa
Source organism: Paenibacillus macerans
Expression system: Escherichia coli
UniProt:
  • Canonical: P23904 (Residues: 26-237; Coverage: 99%)
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 203.68Å b: 42.41Å c: 60.7Å
α: 90° β: 101.27° γ: 90°
R-values:
R R work R free
0.163 not available not available
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structural and sequence-based classification of glycoside hydrolases.
Henrissat et al. (1997)
4 more

6 mentions without citation

Molecular Mechanism by which Prominent Human Gut Bacteroidetes Utilize Mixed-Linkage Beta-Glucans, Major Health-Promoting Cereal Polysaccharides.
Tamura et al. (2017)
5 more