4KF3
Crystal Structure of Myotoxin II (MjTX-II), a myotoxic Lys49-phospholipase A2 from Bothrops moojeni.
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 | 0031640 | biological_process | killing of cells of another organism |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042130 | biological_process | negative regulation of T cell proliferation |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| A | 0050482 | biological_process | arachidonate secretion |
| A | 0050832 | biological_process | defense response to fungus |
| 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 | 0031640 | biological_process | killing of cells of another organism |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042130 | biological_process | negative regulation of T cell proliferation |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| B | 0050482 | biological_process | arachidonate secretion |
| B | 0050832 | biological_process | defense response to fungus |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PE4 B 201 |
| Chain | Residue |
| A | SER1 |
| B | PE4203 |
| B | HOH372 |
| B | HOH374 |
| A | LEU2 |
| A | ILE9 |
| A | TYR22 |
| A | CYS29 |
| A | GLY30 |
| A | LYS70 |
| B | TYR121 |
| B | PRO125 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PE4 B 202 |
| Chain | Residue |
| A | LYS123 |
| A | PRO125 |
| B | LEU2 |
| B | ILE9 |
| B | GLY30 |
| B | CYS45 |
| B | LYS70 |
| B | ARG72 |
| B | HOH385 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PE4 B 203 |
| Chain | Residue |
| A | LEU2 |
| B | GLY23 |
| B | GLY30 |
| B | VAL31 |
| B | GLY32 |
| B | LYS49 |
| B | TYR52 |
| B | PE4201 |
| B | HOH338 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IPA B 204 |
| Chain | Residue |
| B | LYS20 |
| B | LYS115 |
| B | ARG118 |
| B | HOH341 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IPA B 205 |
| Chain | Residue |
| B | ARG34 |
| B | LYS53 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA B 206 |
| Chain | Residue |
| B | ASN17 |
| B | LYS20 |
| B | SER21 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PE4 A 201 |
| Chain | Residue |
| A | PHE3 |
| A | LYS7 |
| A | LEU10 |
| A | GLN11 |
| A | TYR75 |
| A | TRP77 |
| B | LEU10 |
| B | GLN11 |
| B | GLY15 |
| B | TRP77 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IPA A 202 |
| Chain | Residue |
| A | GLY15 |
| A | LYS16 |
| A | ASN17 |
| A | LYS20 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA A 203 |
| Chain | Residue |
| A | GLY33 |
| A | ARG34 |
| A | LYS53 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA A 204 |
| Chain | Residue |
| A | LYS20 |
| A | LYS115 |
| A | ARG118 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | SITE: Cationic membrane-docking site (MDoS) => ECO:0000305|PubMed:29287778 |
| Chain | Residue | Details |
| B | LYS16 | |
| B | LYS20 | |
| A | LYS16 | |
| A | LYS20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6, ECO:0000305|PubMed:29287778 |
| Chain | Residue | Details |
| B | LYS115 | |
| B | ARG118 | |
| A | LYS115 | |
| A | ARG118 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6 |
| Chain | Residue | Details |
| B | LEU122 | |
| B | PHE126 | |
| A | LEU122 | |
| A | PHE126 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6 |
| Chain | Residue | Details |
| B | LYS123 | |
| B | LYS129 | |
| A | LYS123 | |
| A | LYS129 |
