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3QNL

Crystal structure of PrTX-I complexed to Rosmarinic 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
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 IPA A 201
ChainResidue
ATYR22
ACYS29
AGLY30
AIPA202
AHOH381

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA A 202
ChainResidue
AIPA201
AHOH410

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 203
ChainResidue
AHOH411
ALYS115
AARG118

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IPA A 204
ChainResidue
AASN87
AASN88
AGLU108
AHOH394
BIPA203

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ROA A 205
ChainResidue
APHE3
ALYS7
ALEU10
AGLN11
AGLY15
AHOH395
AHOH399
AHOH426
AHOH427
BLYS7
BLEU10
BGLN11
BTRP77
BP33205

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA B 201
ChainResidue
BCYS29
BGLY30
BP33205
BHOH386

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IPA B 202
ChainResidue
BARG72

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA B 203
ChainResidue
AIPA204
AHOH379
BLYS53
BLYS57
BHOH361
BHOH381

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA B 204
ChainResidue
BLYS36
BPRO37
BLYS38

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE P33 B 205
ChainResidue
ALEU10
APRO123
AROA205
BLEU2
BLEU121
BIPA201

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 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 Residues4
DetailsSite: {"description":"Important residue of the cationic membrane-docking site (MDoS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Hydrophobic membrane-disruption site (MDiS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Cationic membrane-docking site (MDoS)","evidences":[{"source":"UniProtKB","id":"I6L8L6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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