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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
A0050482biological_processarachidonate 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
B0050482biological_processarachidonate 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 Residues24
DetailsRegion: {"description":"Important for membrane-damaging activities in eukaryotes and bacteria; heparin-binding","evidences":[{"source":"UniProtKB","id":"P24605","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsSite: {"description":"Putative hydrophobic membrane-disrupting site (MDiS)","evidences":[{"source":"UniProtKB","id":"P20474","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Putative membrane-disrupting site (MDiS)","evidences":[{"source":"UniProtKB","id":"P20474","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Putative cationic membrane-docking site (MDoS)","evidences":[{"source":"UniProtKB","id":"P20474","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important residue of the cationic membrane-docking site (MDoS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Hydrophobic membrane-disruption site (MDiS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Cationic membrane-docking site (MDoS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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