10KU
Structure of hNSP4-S218A bound to MCP3 at 2.09 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008201 | molecular_function | heparin binding |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0051604 | biological_process | protein maturation |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0008201 | molecular_function | heparin binding |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0035578 | cellular_component | azurophil granule lumen |
| B | 0051604 | biological_process | protein maturation |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006508 | biological_process | proteolysis |
| C | 0008201 | molecular_function | heparin binding |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0035578 | cellular_component | azurophil granule lumen |
| C | 0051604 | biological_process | protein maturation |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006508 | biological_process | proteolysis |
| D | 0008201 | molecular_function | heparin binding |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0035578 | cellular_component | azurophil granule lumen |
| D | 0051604 | biological_process | protein maturation |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
| Chain | Residue | Details |
| A | VAL53-CYS58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 916 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"25156428","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PDB","id":"4Q7X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q7Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q7Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q80","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PDB","id":"4Q7Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q7Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q80","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
