4YV5
Crystal Structure of Myotoxin II from Bothrops moojeni complexed to 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 | 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 | arachidonic acid 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 | arachidonic acid 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 | 4 |
Details | binding site for residue SO4 B 201 |
Chain | Residue |
B | LYS20 |
B | LYS115 |
B | ARG118 |
B | SO4202 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 202 |
Chain | Residue |
B | HOH351 |
B | LYS16 |
B | ASN17 |
B | LYS20 |
B | SO4201 |
B | HOH301 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue PE4 B 203 |
Chain | Residue |
A | LYS7 |
A | LEU10 |
A | GLN11 |
A | GLY15 |
A | TYR75 |
A | TRP77 |
B | LYS7 |
B | LEU10 |
B | GLN11 |
B | GLY15 |
B | TYR75 |
B | TRP77 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue 1PE B 204 |
Chain | Residue |
A | TYR121 |
A | LYS123 |
A | PRO125 |
B | LEU2 |
B | ILE9 |
B | CYS29 |
B | GLY30 |
B | HIS48 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 205 |
Chain | Residue |
B | GLY33 |
B | ARG34 |
B | LYS53 |
B | HOH302 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 206 |
Chain | Residue |
A | LYS38 |
A | LYS116 |
A | TYR117 |
B | LYS116 |
B | TYR117 |
site_id | AC7 |
Number of Residues | 30 |
Details | binding site for residue SVR B 207 |
Chain | Residue |
A | PHE3 |
A | LYS7 |
A | LEU10 |
A | ASN17 |
A | PRO18 |
A | CYS27 |
A | LYS38 |
A | ARG72 |
A | PHE126 |
A | CYS127 |
A | LYS128 |
A | SO4202 |
A | SVR205 |
A | HOH380 |
B | ASN114 |
B | LYS115 |
B | LYS116 |
B | TYR119 |
B | TYR121 |
B | LEU122 |
B | PHE126 |
B | HOH305 |
B | HOH311 |
B | HOH316 |
B | HOH320 |
B | HOH338 |
B | HOH347 |
B | HOH352 |
B | HOH356 |
B | HOH361 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 201 |
Chain | Residue |
A | LYS16 |
A | LYS20 |
A | LYS115 |
A | ARG118 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | LYS16 |
A | ASN17 |
A | LYS20 |
A | HOH301 |
B | SVR207 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue 1PE A 203 |
Chain | Residue |
A | ILE9 |
A | PRO18 |
A | TYR22 |
A | ASN28 |
A | GLY30 |
A | CYS45 |
A | HIS48 |
A | LYS49 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | ARG34 |
A | LYS53 |
A | HOH372 |
site_id | AD3 |
Number of Residues | 33 |
Details | binding site for residue SVR A 205 |
Chain | Residue |
A | HOH348 |
A | HOH353 |
A | HOH355 |
A | HOH357 |
A | HOH363 |
A | HOH368 |
A | HOH369 |
B | PHE3 |
B | GLY6 |
B | LYS7 |
B | LEU10 |
B | ASN17 |
B | PRO18 |
B | CYS27 |
B | LYS36 |
B | LYS38 |
B | ARG72 |
B | PHE126 |
B | CYS127 |
B | LYS128 |
B | SVR207 |
B | HOH323 |
B | HOH351 |
A | ASN114 |
A | LYS115 |
A | LYS116 |
A | TYR119 |
A | TYR121 |
A | LEU122 |
A | PHE126 |
A | HOH305 |
A | HOH316 |
A | HOH321 |
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 |