› 1ulo

Solution NMR

N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1ulo/pdb
PDB entry 1ulo coloured by chain, front view.
PDB entry 1ulo coloured by chain, side view.
PDB entry 1ulo coloured by chain, top view.
Source organism: Cellulomonas fimi
Primary publication:
Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy.
Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP
Biochemistry 35 14381-94 (1996)
PMID: 8916925

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146851 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase C Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 15.43 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli
UniProt:
  • Canonical: P14090 (Residues: 33-184; Coverage: 14%)
Gene names: Celf_1537, cenC
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: XPLOR V3.1
Expression system: Escherichia coli

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Citations

6 review citations

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

4 mentions without citation

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