Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-hemolysin translocation ATP-binding protein HlyB
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Peptidase C39 family
Structure domains: Cysteine proteinases
Length: 142 amino acids
Theoretical weight: 16.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q47258 (Residues: 2-137; Coverage: 19%)
Sequence domains: Peptidase C39 family
Structure domains: Cysteine proteinases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
93%
Refinement method:
ARIA
Expression system: Escherichia coli BL21(DE3)
