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 | 8 |
Details | BINDING: BINDING => ECO:0000312|PDB:4BXS |
Chain | Residue | Details |
V | LYS94 | |
V | GLU109 | |
V | ASP112 | |
V | ASP113 | |
V | LYS890 | |
V | PHE905 | |
V | ASP908 | |
V | ASP909 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Not glycosylated => ECO:0000269|PubMed:12730119 |
Chain | Residue | Details |
V | ASN355 | |
V | ASN1367 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by thrombin => ECO:0000250 |
Chain | Residue | Details |
V | ARG742 | |
V | ARG788 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23869089, ECO:0000312|PDB:4BXS |
Chain | Residue | Details |
V | ASN126 | |
V | ASN212 | |
V | ASN376 | |
V | ASN914 | |
V | ASN1150 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
V | ASN174 | |
V | ASN441 | |
V | ASN527 | |
V | ASN971 | |
A | GLU19 | |
A | GLU20 | |
A | GLU25 | |
A | GLU26 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463 |
Chain | Residue | Details |
A | GLU29 | |
A | GLU32 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Hex...) serine => ECO:0000269|PubMed:15351847 |
Chain | Residue | Details |
A | SER52 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15351847 |
Chain | Residue | Details |
A | ASN214 |