› 1gu3

X-ray diffraction
2.3Å resolution

CBM4 structure and function

Released:
DOI: 10.2210/pdb1gu3/pdb
PDB entry 1gu3 coloured by chain, front view.
PDB entry 1gu3 coloured by chain, side view.
PDB entry 1gu3 coloured by chain, top view.
Source organism: Cellulomonas fimi
Primary publication:
Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules.
Boraston AB, Nurizzo D, Notenboom V, Ducros V, Rose DR, Kilburn DG, Davies GJ
J Mol Biol 319 1143-56 (2002)
PMID: 12079353

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146852 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endoglucanase C Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 15.09 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli
UniProt:
  • Canonical: P14090 (Residues: 33-181; Coverage: 14%)
Gene names: Celf_1537, cenC
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 77.634Å b: 77.634Å c: 55.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.209 0.257
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Role of receptors in Bacillus thuringiensis crystal toxin activity.
Pigott et al. (2007)
14 more

11 mentions without citation

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
10 more