6CE2
Crystal structure of Myotoxin I (MjTX-I) from Bothrops moojeni complexed to inhibitor suramin
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 | 9 |
| Details | binding site for residue PE4 A 201 |
| Chain | Residue |
| A | LEU2 |
| A | GLY6 |
| A | PRO18 |
| A | TYR22 |
| A | CYS29 |
| A | GLY30 |
| A | HOH330 |
| B | TYR120 |
| B | SVR202 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue PE4 B 201 |
| Chain | Residue |
| A | PHE125 |
| B | LYS7 |
| B | GLN11 |
| B | TYR75 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | binding site for residue SVR B 202 |
| Chain | Residue |
| A | LEU2 |
| A | GLY30 |
| A | LEU32 |
| A | GLY33 |
| A | ARG34 |
| A | LYS49 |
| A | TYR52 |
| A | PE4201 |
| B | LEU2 |
| B | PRO18 |
| B | TYR22 |
| B | GLY23 |
| B | GLY30 |
| B | LEU32 |
| B | GLY33 |
| B | ARG34 |
| B | LYS49 |
| B | TYR52 |
| B | ASN67 |
| B | PRO68 |
| B | LYS69 |
| B | LYS70 |
| B | HOH301 |
| B | HOH305 |
| B | HOH309 |
| B | HOH321 |
| B | HOH337 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29985425 |
| Chain | Residue | Details |
| B | LYS49 | |
| B | LEU95 | |
| A | GLY35 | |
| A | TYR46 | |
| A | LYS49 | |
| A | LEU95 | |
| B | GLY35 | |
| B | TYR46 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33865953 |
| Chain | Residue | Details |
| A | TYR73 | |
| B | CYS44 | |
| B | ARG72 | |
| B | TYR73 | |
| A | CYS44 | |
| A | ARG72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | SITE: Membrane-docking site (MDoS) => ECO:0000305|PubMed:33865953 |
| Chain | Residue | Details |
| A | TRP77 | |
| A | GLY85 | |
| A | GLU86 | |
| B | CYS50 | |
| B | TYR73 | |
| B | TRP77 | |
| B | GLY85 | |
| B | GLU86 | |
| A | CYS50 | |
| A | TYR73 |
