2Q2J
Crystal structure of PrTX-I, a PLA2 homolog from Bothrops pirajai
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | LYS20 |
| A | LYS115 |
| A | ARG118 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS A 501 |
| Chain | Residue |
| A | LYS16 |
| A | ASN17 |
| A | SER21 |
| A | HOH595 |
| A | HOH635 |
| B | HOH544 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 502 |
| Chain | Residue |
| A | LYS7 |
| A | HOH543 |
| B | GLY15 |
| B | LYS16 |
| B | ASN17 |
| B | LYS20 |
| B | SER21 |
| B | HOH646 |
| B | HOH659 |
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 |
| B | LYS115 | |
| B | ARG118 | |
| A | LYS115 | |
| A | ARG118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6 |
| Chain | Residue | Details |
| B | LEU121 | |
| B | PHE125 | |
| A | LEU121 | |
| A | PHE125 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6 |
| Chain | Residue | Details |
| B | LYS122 | |
| B | LYS129 | |
| A | LYS122 | |
| A | LYS129 |
