4xwn

X-ray diffraction
2.88Å resolution

Complex structure of catalytic domain of Clostridium Cellulovorans Exgs and Cellotetraose

Released:
Source organism: Clostridium cellulovorans
Primary publication:
Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.
Acta Crystallogr F Struct Biol Commun 71 1264-72 (2015)
PMID: 26457517

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Dockerin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 681 amino acids
Theoretical weight: 75.89 KDa
Source organism: Clostridium cellulovorans
Expression system: Escherichia coli
UniProt:
  • Canonical: O65986 (Residues: 32-674; Coverage: 92%)
Gene name: exgS
Sequence domains: Glycosyl hydrolase family 48
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer : NEW Components: BGC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1, NSRRC BEAMLINE BL13C1
Spacegroup: P41212
Unit cell:
a: 108.856Å b: 108.856Å c: 182.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.193
Expression system: Escherichia coli