› 1ut9

X-ray diffraction
2.1Å resolution

Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum

Released:
DOI: 10.2210/pdb1ut9/pdb
PDB entry 1ut9 coloured by chain, front view.
PDB entry 1ut9 coloured by chain, side view.
PDB entry 1ut9 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum.
Schubot FD, Kataeva IA, Chang J, Shah AK, Ljungdahl LG, Rose JP, Wang BC
Biochemistry 43 1163-70 (2004)
PMID: 14756552

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoglucanase Chain: A
Molecule details ›
Chain: A
Length: 609 amino acids
Theoretical weight: 68.61 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6RSN8 (Residues: 2-607; Coverage: 100%)
Gene name: cbhA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P212121
Unit cell:
a: 74.546Å b: 75.76Å c: 137.498Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Thermophilic lignocellulose deconstruction.
Blumer-Schuette et al. (2014)
3 more

5 mentions without citation

Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution.
Omelchenko et al. (2010)
4 more