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 ›
Chains: A, C
Length: 151 amino acids
Theoretical weight: 15.56 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli BL21(DE3)
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 BL21(DE3)
UniProt:
- Canonical:
Q45996 (Residues: 277-427; Coverage: 10%)
Sequence domains: Cohesin domain
Structure domains: Immunoglobulin-like
Endoglucanase A
Molecule details ›
Chains: B, D
Length: 66 amino acids
Theoretical weight: 7.29 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Dockerin type I domain
Structure domains: Dockerin domain
Length: 66 amino acids
Theoretical weight: 7.29 KDa
Source organism: Ruminiclostridium cellulolyticum
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P17901 (Residues: 410-475; Coverage: 15%)
Sequence domains: Dockerin type I domain
Structure domains: Dockerin domain
