3UIR
Crystal structure of the plasmin-textilinin-1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0030414 | molecular_function | peptidase inhibitor activity |
| C | 0044469 | biological_process | venom-mediated blood coagulation |
| C | 0044483 | biological_process | venom-mediated perturbation of hemostasis |
| C | 0090729 | molecular_function | toxin activity |
| D | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0030414 | molecular_function | peptidase inhibitor activity |
| D | 0044469 | biological_process | venom-mediated blood coagulation |
| D | 0044483 | biological_process | venom-mediated perturbation of hemostasis |
| D | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 801 |
| Chain | Residue |
| B | ARG712 |
| B | TYR713 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 101 |
| Chain | Residue |
| D | THR49 |
| D | LYS50 |
| D | GLU51 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| A | LEU599-CYS604 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV |
| Chain | Residue | Details |
| A | ASP735-VAL746 |
| site_id | PS00280 |
| Number of Residues | 19 |
| Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCegnannFitkeeC |
| Chain | Residue | Details |
| C | PHE35-CYS53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 454 |
| 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 | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9201958","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 100 |
| Details | Domain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Reactive bond for trypsin","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 425 |
| Chain | Residue | Details |
| A | HIS603 | proton shuttle (general acid/base) |
| A | ASP646 | electrostatic stabiliser, modifies pKa |
| A | SER741 | covalent catalysis, proton shuttle (general acid/base) |
| A | GLY742 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 425 |
| Chain | Residue | Details |
| B | HIS603 | proton shuttle (general acid/base) |
| B | ASP646 | electrostatic stabiliser, modifies pKa |
| B | SER741 | covalent catalysis, proton shuttle (general acid/base) |
| B | GLY742 | electrostatic stabiliser |
