› 1glh

X-ray diffraction
2Å resolution

CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY

Released:
DOI: 10.2210/pdb1glh/pdb
PDB entry 1glh coloured by chain, front view.
PDB entry 1glh coloured by chain, side view.
PDB entry 1glh coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability.
Keitel T, Meldgaard M, Heinemann U
Eur J Biochem 222 203-14 (1994)
PMID: 8200344

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 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.94 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: P23904 (Residues: 25-237; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 16
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 70.22Å b: 72.56Å c: 49.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 not available 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
Planas A. (2000)
1 more

2 mentions without citation

Topology independent protein structural alignment.
Dundas et al. (2007)
1 more