Function and Biology Details
Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Cellulase (preferred)
PDBe Complex ID:
PDB-CPX-192867 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellulase
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 10.91 KDa
Source organism: Piromyces sp. 'equi'
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Cellulose or protein binding domain
Structure domains: Cellulose docking domain, dockering
Length: 100 amino acids
Theoretical weight: 10.91 KDa
Source organism: Piromyces sp. 'equi'
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9P868 (Residues: 19-118; Coverage: 25%)
Sequence domains: Cellulose or protein binding domain
Structure domains: Cellulose docking domain, dockering
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
96%
Refinement method:
CNS
Expression system: Escherichia coli BL21
