PDBe 1cel

X-ray diffraction
1.8Å resolution

THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI

Released:

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
Macromolecule:
Exoglucanase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 434 amino acids
Theoretical weight: 46.01 KDa
Source organism: Trichoderma reesei
Expression system: Not provided
UniProt:
  • Canonical: P62694 (Residues: 18-451; Coverage: 88%)
Gene name: cbh1
Sequence domains: Glycosyl hydrolase family 7
Structure domains: 1,4-Beta-D-Glucan Cellobiohydrolase I, subunit A

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 84Å b: 86.2Å c: 111.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Not provided