Function and Biology Details
Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Endo-1,4-beta-xylanase C (preferred)
PDBe Complex ID:
PDB-CPX-130646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Endo-1,4-beta-xylanase C
Molecule details ›
Chains: A, B, C
Length: 181 amino acids
Theoretical weight: 19.92 KDa
Source organism: Paenibacillus barcinonensis
Expression system: Escherichia coli
UniProt:
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like
Length: 181 amino acids
Theoretical weight: 19.92 KDa
Source organism: Paenibacillus barcinonensis
Expression system: Escherichia coli
UniProt:
- Canonical:
O69230 (Residues: 186-366; Coverage: 17%)
Sequence domains: Carbohydrate binding domain
Structure domains: Galactose-binding domain-like
Ligands and Environments
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-2
Spacegroup:
P32
Expression system: Escherichia coli
