3QNL
Crystal structure of PrTX-I complexed to Rosmarinic Acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004623 | molecular_function | phospholipase A2 activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005543 | molecular_function | phospholipid binding |
A | 0005576 | cellular_component | extracellular region |
A | 0006644 | biological_process | phospholipid metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0042130 | biological_process | negative regulation of T cell proliferation |
A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
A | 0050482 | biological_process | arachidonic acid secretion |
A | 0090729 | molecular_function | toxin activity |
B | 0004623 | molecular_function | phospholipase A2 activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005543 | molecular_function | phospholipid binding |
B | 0005576 | cellular_component | extracellular region |
B | 0006644 | biological_process | phospholipid metabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0042130 | biological_process | negative regulation of T cell proliferation |
B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
B | 0050482 | biological_process | arachidonic acid secretion |
B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 201 |
Chain | Residue |
A | TYR22 |
A | CYS29 |
A | GLY30 |
A | IPA202 |
A | HOH381 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA A 202 |
Chain | Residue |
A | IPA201 |
A | HOH410 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA A 203 |
Chain | Residue |
A | HOH411 |
A | LYS115 |
A | ARG118 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 204 |
Chain | Residue |
A | ASN87 |
A | ASN88 |
A | GLU108 |
A | HOH394 |
B | IPA203 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ROA A 205 |
Chain | Residue |
A | PHE3 |
A | LYS7 |
A | LEU10 |
A | GLN11 |
A | GLY15 |
A | HOH395 |
A | HOH399 |
A | HOH426 |
A | HOH427 |
B | LYS7 |
B | LEU10 |
B | GLN11 |
B | TRP77 |
B | P33205 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IPA B 201 |
Chain | Residue |
B | CYS29 |
B | GLY30 |
B | P33205 |
B | HOH386 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IPA B 202 |
Chain | Residue |
B | ARG72 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA B 203 |
Chain | Residue |
A | IPA204 |
A | HOH379 |
B | LYS53 |
B | LYS57 |
B | HOH361 |
B | HOH381 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA B 204 |
Chain | Residue |
B | LYS36 |
B | PRO37 |
B | LYS38 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE P33 B 205 |
Chain | Residue |
A | LEU10 |
A | PRO123 |
A | ROA205 |
B | LEU2 |
B | LEU121 |
B | IPA201 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | SITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6 |
Chain | Residue | Details |
A | LYS115 | |
A | ARG118 | |
B | LYS115 | |
B | ARG118 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6 |
Chain | Residue | Details |
A | LEU121 | |
A | PHE125 | |
B | LEU121 | |
B | PHE125 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6 |
Chain | Residue | Details |
A | LYS122 | |
A | LYS129 | |
B | LYS122 | |
B | LYS129 |