8COY
Structure of the catalytic domain of P. vivax Sub1 (triclinic crystal form) in complex with inhibitor
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 | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240 |
| Chain | Residue | Details |
| A | ASP316 | |
| A | HIS372 | |
| A | SER549 | |
| B | ASP316 | |
| B | HIS372 | |
| B | SER549 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25204226, ECO:0000269|PubMed:37428845, ECO:0000269|PubMed:38503166, ECO:0007744|PDB:4TR2, ECO:0007744|PDB:8COY, ECO:0007744|PDB:8COZ, ECO:0007744|PDB:8QKE, ECO:0007744|PDB:8QKG |
| Chain | Residue | Details |
| A | ASP281 | |
| A | VAL350 | |
| A | ASP352 | |
| A | ASP353 | |
| A | VAL383 | |
| A | ILE388 | |
| A | ILE390 | |
| B | ASP281 | |
| B | ASP325 | |
| B | GLU336 | |
| B | ARG340 | |
| A | ASP325 | |
| B | VAL343 | |
| B | ASP344 | |
| B | ASP345 | |
| B | ASP346 | |
| B | ASN348 | |
| B | VAL350 | |
| B | ASP352 | |
| B | ASP353 | |
| B | VAL383 | |
| B | ILE388 | |
| A | GLU336 | |
| B | ILE390 | |
| A | ARG340 | |
| A | VAL343 | |
| A | ASP344 | |
| A | ASP345 | |
| A | ASP346 | |
| A | ASN348 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25204226, ECO:0000269|PubMed:37428845, ECO:0000269|PubMed:38503166, ECO:0007744|PDB:4TR2, ECO:0007744|PDB:8COY, ECO:0007744|PDB:8COZ, ECO:0007744|PDB:8QKG |
| Chain | Residue | Details |
| A | ASN386 | |
| B | ASN386 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Cleavage => ECO:0000269|PubMed:37428845 |
| Chain | Residue | Details |
| A | ALA357 | |
| B | ALA357 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:37428845, ECO:0000269|PubMed:38503166, ECO:0007744|PDB:8COY, ECO:0007744|PDB:8COZ, ECO:0007744|PDB:8QKE, ECO:0007744|PDB:8QKG |
| Chain | Residue | Details |
| A | ASN546 | |
| B | ASN546 |
