Function and Biology Details
Reaction catalysed:
Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oligoxyloglucan reducing end-specific cellobiohydrolase
Molecule details ›
Chains: A, B
Length: 789 amino acids
Theoretical weight: 84.97 KDa
Source organism: Geotrichum sp. M128
Expression system: Escherichia coli
UniProt:
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Length: 789 amino acids
Theoretical weight: 84.97 KDa
Source organism: Geotrichum sp. M128
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8J0D2 (Residues: 24-812; Coverage: 100%)
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-18B
Spacegroup:
P212121
Expression system: Escherichia coli
