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4BXW

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
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016504molecular_functionpeptidase activator activity
B0016787molecular_functionhydrolase activity
B0032991cellular_componentprotein-containing complex
B0044469biological_processvenom-mediated blood coagulation
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1412
ChainResidue
ATYR350
AASP351
AARG388
ALYS391

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1413
ChainResidue
BVAL295
BCYS89
BARG90
BASP92
BASN93
BGLN294

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1414
ChainResidue
BASN293
BGLN294
BLYS298

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1413
ChainResidue
ATYR262
A0GJ1411

site_idAC5
Number of Residues17
DetailsBinding site for Ligand 0GJ A1411 bound to SER A 362
ChainResidue
AHIS211
ATYR262
AASP356
AALA357
ACYS358
AGLN359
AGLY360
ASER362
ASER381
ASER382
AGLY383
AGLY385
AGLY393
AGOL1413
AHOH2063
AHOH2081
AHOH2086

site_idAC6
Number of Residues16
DetailsBinding site for Ligand 0GJ B1412 bound to SER B 362
ChainResidue
BHIS211
BTYR262
BASP356
BALA357
BCYS358
BGLN359
BGLY360
BSER362
BSER381
BSER382
BGLY383
BGLY385
BGLY393
BHOH2019
BHOH2062
BHOH2063

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_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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15351847","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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