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5VFM

Crystal structure of BnSP-7 from Bothrops pauloensis complexed with p-coumaric 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
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
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
B0042742biological_processdefense response to bacterium
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ME2 B 201
ChainResidue
ALEU121
BLEU2
BGLY6
BALA19

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 B 202
ChainResidue
BLYS16
BASN17
BLYS20
BSO4203
BHOH305

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 B 203
ChainResidue
BLYS16
BLYS20
BLYS115
BARG118
BSO4202

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 204
ChainResidue
BGLY33
BARG34
BLYS53
BHOH309

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 B 205
ChainResidue
BGLU4
BLYS7
BARG72
BTYR73
BHOH303
BHOH324

site_idAC6
Number of Residues3
Detailsbinding site for residue ME2 A 201
ChainResidue
ALEU2
AGLY6
AHOH378

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 202
ChainResidue
ALYS16
AASN17
AHC4207
AHOH304

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 A 203
ChainResidue
AGLY33
AARG34

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 A 204
ChainResidue
APRO37
AARG43
AHOH352

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 A 205
ChainResidue
AILE104
AARG107
AHOH313
AHOH338
AHOH342
AHOH351

site_idAD2
Number of Residues4
Detailsbinding site for residue SO4 A 206
ChainResidue
ACYS51
ALYS57
AHOH306
AHOH308

site_idAD3
Number of Residues7
Detailsbinding site for residue HC4 A 207
ChainResidue
ALYS16
ALYS20
ALYS115
AARG118
ATYR119
ASO4202
BLYS20

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
BCYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
BLEU95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000305|PubMed:28751219
ChainResidueDetails
BASN17
AASN17

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:28751219
ChainResidueDetails
BLYS20
ALYS20

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:28751219
ChainResidueDetails
BLYS115
BARG118
ALYS115
AARG118

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:28751219
ChainResidueDetails
BLEU121
BPHE125
ALEU121
APHE125

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PDB entries from 2024-07-10

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