Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Subtilisin-like protease 2 (preferred)
PDBe Complex ID:
PDB-CPX-132183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin-like protease 2
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 17.72 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
Sequence domains: Prodomain subtilisin 2
Structure domains: Alpha-Beta Plaits
Length: 149 amino acids
Theoretical weight: 17.72 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
- Canonical:
O97364 (Residues: 530-676; Coverage: 11%)
Sequence domains: Prodomain subtilisin 2
Structure domains: Alpha-Beta Plaits
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
63%
Refinement method:
simulated annealing
Expression system: Escherichia coli
