4BXW
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 | 0006508 | biological_process | proteolysis |
| A | 0007596 | biological_process | blood coagulation |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016504 | molecular_function | peptidase activator activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0035807 | biological_process | induction of blood coagulation in another organism |
| A | 0044469 | biological_process | envenomation resulting in positive regulation of blood coagulation in another organism |
| A | 0090729 | molecular_function | toxin activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0007596 | biological_process | blood coagulation |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0016504 | molecular_function | peptidase activator activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0035807 | biological_process | induction of blood coagulation in another organism |
| B | 0044469 | biological_process | envenomation resulting in positive regulation of blood coagulation in another organism |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1412 |
| Chain | Residue |
| A | TYR350 |
| A | ASP351 |
| A | ARG388 |
| A | LYS391 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1413 |
| Chain | Residue |
| B | VAL295 |
| B | CYS89 |
| B | ARG90 |
| B | ASP92 |
| B | ASN93 |
| B | GLN294 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1414 |
| Chain | Residue |
| B | ASN293 |
| B | GLN294 |
| B | LYS298 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1413 |
| Chain | Residue |
| A | TYR262 |
| A | 0GJ1411 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | Binding site for Ligand 0GJ A1411 bound to SER A 362 |
| Chain | Residue |
| A | HIS211 |
| A | TYR262 |
| A | ASP356 |
| A | ALA357 |
| A | CYS358 |
| A | GLN359 |
| A | GLY360 |
| A | SER362 |
| A | SER381 |
| A | SER382 |
| A | GLY383 |
| A | GLY385 |
| A | GLY393 |
| A | GOL1413 |
| A | HOH2063 |
| A | HOH2081 |
| A | HOH2086 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | Binding site for Ligand 0GJ B1412 bound to SER B 362 |
| Chain | Residue |
| B | HIS211 |
| B | TYR262 |
| B | ASP356 |
| B | ALA357 |
| B | CYS358 |
| B | GLN359 |
| B | GLY360 |
| B | SER362 |
| B | SER381 |
| B | SER382 |
| B | GLY383 |
| B | GLY385 |
| B | GLY393 |
| B | HOH2019 |
| B | HOH2062 |
| B | HOH2063 |
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 | 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Charge relay system => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS211 | |
| A | ILE269 | |
| A | HIS366 | |
| B | HIS211 | |
| B | ILE269 | |
| B | HIS366 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Not modified => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU35 | |
| B | GLU35 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Not modified |
| Chain | Residue | Details |
| A | ASP63 | |
| B | ASP63 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Cleavage |
| Chain | Residue | Details |
| A | ARG169 | |
| B | ARG169 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232 |
| Chain | Residue | Details |
| A | GLU6 | |
| B | GLU7 | |
| B | GLU14 | |
| B | GLU16 | |
| B | GLU19 | |
| B | GLU20 | |
| B | GLU25 | |
| B | GLU26 | |
| A | GLU7 | |
| A | GLU14 | |
| A | GLU16 | |
| A | GLU19 | |
| A | GLU20 | |
| A | GLU25 | |
| A | GLU26 | |
| B | GLU6 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463 |
| Chain | Residue | Details |
| A | GLU29 | |
| A | GLU32 | |
| B | GLU29 | |
| B | GLU32 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (Hex...) serine => ECO:0000269|PubMed:15351847 |
| Chain | Residue | Details |
| A | SER52 | |
| B | SER52 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15351847 |
| Chain | Residue | Details |
| A | ASN214 | |
| B | ASN214 |
