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
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148210 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CBM3 domain-containing protein
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 15.56 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli
UniProt:
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like
Length: 151 amino acids
Theoretical weight: 15.56 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q45996 (Residues: 277-427; Coverage: 10%)
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like
Endoglucanase A
Molecule details ›
Chain: B
Length: 64 amino acids
Theoretical weight: 7.15 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli
UniProt:
Sequence domains: Dockerin type I domain
Structure domains: Dockerin domain
Length: 64 amino acids
Theoretical weight: 7.15 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli
UniProt:
- Canonical: P17901 (Residues: 410-473; Coverage: 14%)
Sequence domains: Dockerin type I domain
Structure domains: Dockerin domain
