Function and Biology Details
Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glycoside hydrolase family 11
- Aspartic peptidase domain superfamily
- Glycosyl hydrolase 11 domain
- Glycoside hydrolase family 11, active site 2
- Glycoside hydrolase family 11, active site 1
- Concanavalin A-like lectin/glucanase domain superfamily
- Glycoside hydrolase family 11/12
- Xylanase inhibitor, C-terminal
4 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148367 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase A1 domain-containing protein
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 38.85 KDa
Source organism: Triticum aestivum
UniProt:
Sequence domains:
Structure domains: Acid Proteases
Length: 381 amino acids
Theoretical weight: 38.85 KDa
Source organism: Triticum aestivum
UniProt:
- Canonical:
Q8H0K8 (Residues: 22-402; Coverage: 100%)
Sequence domains:
Structure domains: Acid Proteases
Endo-1,4-beta-xylanase A
Molecule details ›
Chain: B
Length: 185 amino acids
Theoretical weight: 20.41 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls
Length: 185 amino acids
Theoretical weight: 20.41 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
- Canonical: P18429 (Residues: 29-213; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
ESRF BEAMLINE ID14-1
Spacegroup:
C2
Expression system: Escherichia coli
