9FM5
PvSub1 Catalytic Domain in Complex with Peptidomimetic Inhibitor (AL-97)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. ICVIDSGIdynH |
| Chain | Residue | Details |
| A | ILE312-HIS323 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVSGiISA |
| Chain | Residue | Details |
| A | HIS372-ALA382 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAA |
| Chain | Residue | Details |
| A | GLY547-ALA557 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25204226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TR2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25204226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TR2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38503166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8COY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8COZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QKG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 317 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"37428845","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
