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1PC9

Crystal Structure of BnSP-6, a Lys49-Phospholipase A2

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_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
B0042742biological_processdefense response to bacterium
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonate secretion
B0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYvHKcC
ChainResidueDetails
ACYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAVaIC
ChainResidueDetails
ALEU95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000305|PubMed:28751219
ChainResidueDetails
AALA19
BALA19

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:28751219
ChainResidueDetails
ATYR22
BTYR22

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
ATYR117
AHIS120
BTYR117
BHIS120

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:28751219
ChainResidueDetails
APRO123
ALYS127
BPRO123
BLYS127

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP99

226707

PDB entries from 2024-10-30

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