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6B83

Crystal structure of Myotoxin II from Bothrops moojeni complexed to Caproic acid

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
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0042742biological_processdefense response to bacterium
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0050832biological_processdefense response to fungus
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
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0042742biological_processdefense response to bacterium
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0050832biological_processdefense response to fungus
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue 6NA B 201
ChainResidue
BTYR21
BCYS28
BGLY29
BHIS47
BHOH345

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 B 202
ChainResidue
BHOH313
BHOH340
BHOH346
BLYS15
BASN16
BLYS19
BHOH304

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 B 203
ChainResidue
BGLY32
BARG33
BLYS52
BHOH347
BHOH360
BHOH384

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 204
ChainResidue
BLYS15
BLYS19
BLYS105
BARG108

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 201
ChainResidue
ALYS15
AASN16
ALYS19
AHOH305
AHOH311

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 202
ChainResidue
ALYS15
ALYS19
ALYS105
AARG108

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 203
ChainResidue
AGLY32
AARG33
AHOH352

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 204
ChainResidue
AASN104
ALYS106
AHOH369
BLYS35

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
BCYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
BLEU85-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000305|PubMed:29287778
ChainResidueDetails
BLYS15
BLYS19
ALYS15
ALYS19

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:29287778
ChainResidueDetails
BLYS105
BARG108
ALYS105
AARG108

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
BLEU112
BALA115
ALEU112
AALA115

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6
ChainResidueDetails
BLYS113
BLYS118
ALYS113
ALYS118

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PDB entries from 2024-05-15

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