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7LYE

Myotoxin I from Bothrops moojeni co-crystallized with synthetic inhibitor Varespladib (LY315920)

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
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0035821biological_processmodulation of process of another organism
C0042130biological_processnegative regulation of T cell proliferation
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonic acid secretion
C0090729molecular_functiontoxin activity
D0004623molecular_functionphospholipase A2 activity
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0006644biological_processphospholipid metabolic process
D0016042biological_processlipid catabolic process
D0035821biological_processmodulation of process of another organism
D0042130biological_processnegative regulation of T cell proliferation
D0047498molecular_functioncalcium-dependent phospholipase A2 activity
D0050482biological_processarachidonic acid secretion
D0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
ALEU85-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:29985425
ChainResidueDetails
AVAL18
CGLY29
CGLY32
CLYS69
DVAL18
DGLY29
DGLY32
DLYS69
AGLY29
AGLY32
ALYS69
BVAL18
BGLY29
BGLY32
BLYS69
CVAL18

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:33865953
ChainResidueDetails
AASN27
DASN27
DHIS47
DLYS48
AHIS47
ALYS48
BASN27
BHIS47
BLYS48
CASN27
CHIS47
CLYS48

site_idSWS_FT_FI3
Number of Residues28
DetailsSITE: Membrane-docking site (MDoS) => ECO:0000305|PubMed:33865953
ChainResidueDetails
AARG33
BLYS52
BLYS60
BLYS61
BLYS113
BLYS118
CARG33
CLYS48
CLYS52
CLYS60
CLYS61
ALYS48
CLYS113
CLYS118
DARG33
DLYS48
DLYS52
DLYS60
DLYS61
DLYS113
DLYS118
ALYS52
ALYS60
ALYS61
ALYS113
ALYS118
BARG33
BLYS48

site_idSWS_FT_FI4
Number of Residues8
DetailsSITE: Membrane-disrupting site (MDiS) => ECO:0000305|PubMed:33865953
ChainResidueDetails
ALEU112
APHE115
BLEU112
BPHE115
CLEU112
CPHE115
DLEU112
DPHE115

222415

PDB entries from 2024-07-10

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