Function and Biology Details
Reaction catalysed:
Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
Beta-1,3-xylanase (preferred)
PDBe Complex ID:
PDB-CPX-186033 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-1,3-xylanase
Molecule details ›
Chains: D, E, F, G, H, I
Length: 104 amino acids
Theoretical weight: 12.16 KDa
Source organism: Alcaligenes sp. XY-234
Expression system: Escherichia coli
UniProt:
Sequence domains: Family 31 carbohydrate binding protein
Structure domains: Beta-1,3-xylanase, CBM31 domain
Length: 104 amino acids
Theoretical weight: 12.16 KDa
Source organism: Alcaligenes sp. XY-234
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8RS40 (Residues: 375-469; Coverage: 21%)
Sequence domains: Family 31 carbohydrate binding protein
Structure domains: Beta-1,3-xylanase, CBM31 domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL45PX
Spacegroup:
P212121
Expression system: Escherichia coli
