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3JR8

Crystal Structure of BthTX-II (Asp49-PLA2 from Bothrops jararacussu snake venom) with calcium ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 134
ChainResidue
BTYR22
BTHR41
BPHE106
BASN109
BLEU110

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 135
ChainResidue
BASP39
BALA40
BTHR41
BTHR112

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 134
ChainResidue
ATYR22
ATHR41
APHE106
ALEU110
ATYR113

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 135
ChainResidue
AASP39
ATHR41
AASN109
ATHR112

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCFvHDcC
ChainResidueDetails
ACYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaVC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsSITE: Putative hydrophobic membrane-disrupting site (MDiS) => ECO:0000250|UniProtKB:P20474
ChainResidueDetails
ATRP3
ALEU10
ALEU17
BTRP3
BLEU10
BLEU17

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Putative membrane-disrupting site (MDiS) => ECO:0000250|UniProtKB:P20474
ChainResidueDetails
ALYS16
BLYS16

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Putative cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:P20474
ChainResidueDetails
AARG72
BARG72

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
ALYS115
BLYS115

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
ALEU125
BLEU125

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
ALYS128
BLYS128

221051

PDB entries from 2024-06-12

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