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4BXS

Crystal Structure of the Prothrombinase Complex from the Venom of Pseudonaja Textilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016504molecular_functionpeptidase activator activity
A0016787molecular_functionhydrolase activity
A0032991cellular_componentprotein-containing complex
A0044469biological_processvenom-mediated blood coagulation
A0090729molecular_functiontoxin activity
V0004252molecular_functionserine-type endopeptidase activity
V0005507molecular_functioncopper ion binding
V0005515molecular_functionprotein binding
V0005576cellular_componentextracellular region
V0005886cellular_componentplasma membrane
V0016504molecular_functionpeptidase activator activity
V0032991cellular_componentprotein-containing complex
V0038023molecular_functionsignaling receptor activity
V0044469biological_processvenom-mediated blood coagulation
V0046872molecular_functionmetal ion binding
V0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDgigsYtCtC
ChainResidueDetails
ACYS61-CYS72

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EciEErCskeearEvfeddektet.FW
ChainResidueDetails
AGLU16-TRP41

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtClsGyeGKnC
ChainResidueDetails
ACYS70-CYS81

site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWlIsSlVAkhLqAGMygyL
ChainResidueDetails
VGLY277-LEU297
VGLY632-PHE652
VGLY1090-PHE1110

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU207-CYS212

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHT
ChainResidueDetails
AASP356-THR367

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtClsGYegkn....C
ChainResidueDetails
ACYS70-CYS81
ACYS109-CYS124

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCssnp..........Chyrgi..CkDgigsYtC
ChainResidueDetails
AASP46-CYS70

site_idPS01285
Number of Residues31
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsiikkehehp.....WIqIDlqrqvvItgIqTQG
ChainResidueDetails
VALA1157-GLY1187
VALA1317-GLY1346

site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Pktwnqyia..LRiELfGC
ChainResidueDetails
VPRO1411-CYS1427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000312|PDB:4BXS
ChainResidueDetails
VLYS94
VGLU109
VASP112
VASP113
VLYS890
VPHE905
VASP908
VASP909

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:12730119
ChainResidueDetails
VASN355
VASN1367

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by thrombin => ECO:0000250
ChainResidueDetails
VARG742
VARG788

site_idSWS_FT_FI4
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23869089, ECO:0000312|PDB:4BXS
ChainResidueDetails
VASN126
VASN212
VASN376
VASN914
VASN1150

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
VASN174
VASN441
VASN527
VASN971
AGLU19
AGLU20
AGLU25
AGLU26

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463
ChainResidueDetails
AGLU29
AGLU32

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: O-linked (Hex...) serine => ECO:0000269|PubMed:15351847
ChainResidueDetails
ASER52

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15351847
ChainResidueDetails
AASN214

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PDB entries from 2025-06-11

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