Function and Biology Details
Reaction catalysed:
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose andcellotetraose, releasing cellobiose from the non-reducing ends of thechains.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
CBM2 domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-175290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
CBM2 domain-containing protein
Molecule details ›
Chain: A
Length: 642 amino acids
Theoretical weight: 71.76 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
UniProt:
Sequence domains: Glycosyl hydrolase family 48
Structure domains:
Length: 642 amino acids
Theoretical weight: 71.76 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
UniProt:
- Canonical:
Q47NH7 (Residues: 343-984; Coverage: 68%)
Sequence domains: Glycosyl hydrolase family 48
Structure domains:
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
BRUKER AXS MICROSTAR
Spacegroup:
P21
Expression system: Escherichia coli
