› 2vi0

X-ray diffraction
1.51Å resolution

Lichenase CtLic26 in complex with a thio-oligosaccharide

Released:
DOI: 10.2210/pdb2vi0/pdb
PDB entry 2vi0 coloured by chain, front view.
PDB entry 2vi0 coloured by chain, side view.
PDB entry 2vi0 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.
Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ
Org Biomol Chem 6 851-3 (2008)
PMID: 18292875

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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Endoglucanase H Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 32.05 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P16218 (Residues: 26-304; Coverage: 30%)
Gene names: Cthe_1472, celH
Sequence domains: Glycosyl hydrolase family 26
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: MGL, SGC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 49.578Å b: 62.648Å c: 79.067Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.189
Expression system: Escherichia coli BL21

Quick links

Citations

1 citations in other articles

Understanding how noncatalytic carbohydrate binding modules can display specificity for xyloglucan.
Luís et al. (2013)

1 mention without citation

End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.
Sine SM. (2012)