4BXS
Crystal Structure of the Prothrombinase Complex from the Venom of Pseudonaja Textilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0007596 | biological_process | blood coagulation |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016504 | molecular_function | peptidase activator activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0044469 | biological_process | venom-mediated blood coagulation |
| A | 0090729 | molecular_function | toxin activity |
| V | 0004252 | molecular_function | serine-type endopeptidase activity |
| V | 0005507 | molecular_function | copper ion binding |
| V | 0005515 | molecular_function | protein binding |
| V | 0005576 | cellular_component | extracellular region |
| V | 0005886 | cellular_component | plasma membrane |
| V | 0016504 | molecular_function | peptidase activator activity |
| V | 0032991 | cellular_component | protein-containing complex |
| V | 0038023 | molecular_function | signaling receptor activity |
| V | 0044469 | biological_process | venom-mediated blood coagulation |
| V | 0046872 | molecular_function | metal ion binding |
| V | 0090729 | molecular_function | toxin activity |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDgigsYtCtC |
| Chain | Residue | Details |
| A | CYS61-CYS72 |
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EciEErCskeearEvfeddektet.FW |
| Chain | Residue | Details |
| A | GLU16-TRP41 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtClsGyeGKnC |
| Chain | Residue | Details |
| A | CYS70-CYS81 |
| site_id | PS00079 |
| Number of Residues | 21 |
| Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWlIsSlVAkhLqAGMygyL |
| Chain | Residue | Details |
| V | GLY277-LEU297 | |
| V | GLY632-PHE652 | |
| V | GLY1090-PHE1110 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| A | LEU207-CYS212 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHT |
| Chain | Residue | Details |
| A | ASP356-THR367 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtClsGYegkn....C |
| Chain | Residue | Details |
| A | CYS70-CYS81 | |
| A | CYS109-CYS124 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCssnp..........Chyrgi..CkDgigsYtC |
| Chain | Residue | Details |
| A | ASP46-CYS70 |
| site_id | PS01285 |
| Number of Residues | 31 |
| Details | FA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsiikkehehp.....WIqIDlqrqvvItgIqTQG |
| Chain | Residue | Details |
| V | ALA1157-GLY1187 | |
| V | ALA1317-GLY1346 |
| site_id | PS01286 |
| Number of Residues | 17 |
| Details | FA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Pktwnqyia..LRiELfGC |
| Chain | Residue | Details |
| V | PRO1411-CYS1427 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15351847","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 124 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 146 |
| Details | Domain: {"description":"Plastocyanin-like 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 154 |
| Details | Domain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4BXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"12730119","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23869089","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
