4GV5
X-ray structure of crotamine, a cell-penetrating peptide from the Brazilian snake Crotalus durissus terrificus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0015459 | molecular_function | potassium channel regulator activity |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044564 | biological_process | envenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism |
A | 0050832 | biological_process | defense response to fungus |
A | 0090729 | molecular_function | toxin activity |
B | 0005576 | cellular_component | extracellular region |
B | 0015459 | molecular_function | potassium channel regulator activity |
B | 0031640 | biological_process | killing of cells of another organism |
B | 0042742 | biological_process | defense response to bacterium |
B | 0044564 | biological_process | envenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism |
B | 0050832 | biological_process | defense response to fungus |
B | 0090729 | molecular_function | toxin activity |
C | 0005576 | cellular_component | extracellular region |
C | 0015459 | molecular_function | potassium channel regulator activity |
C | 0031640 | biological_process | killing of cells of another organism |
C | 0042742 | biological_process | defense response to bacterium |
C | 0044564 | biological_process | envenomation resulting in occlusion of the pore of voltage-gated potassium channel in another organism |
C | 0050832 | biological_process | defense response to fungus |
C | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SCN A 101 |
Chain | Residue |
A | ILE17 |
A | HOH204 |
C | TYR1 |
C | TRP34 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SCN A 102 |
Chain | Residue |
A | PRO13 |
A | LYS14 |
A | GLU15 |
B | PRO21 |
C | PRO13 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 103 |
Chain | Residue |
A | LYS14 |
A | TRP32 |
A | ARG33 |
B | PRO21 |
B | SER22 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 104 |
Chain | Residue |
A | GLN3 |
A | TRP32 |
A | ARG33 |
A | HOH215 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 101 |
Chain | Residue |
B | LYS2 |
B | GLN3 |
B | TRP32 |
B | ARG33 |
B | HOH209 |
B | HOH211 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 102 |
Chain | Residue |
B | TYR1 |
B | HIS10 |
B | CYS11 |
B | HOH213 |
C | ARG31 |
C | TRP32 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SCN B 103 |
Chain | Residue |
B | PHE12 |
B | PRO13 |
B | ILE17 |
B | GLY42 |
C | GOL103 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 101 |
Chain | Residue |
A | PHE12 |
A | PRO13 |
A | LYS16 |
C | HIS10 |
C | CYS11 |
C | HOH204 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SCN C 102 |
Chain | Residue |
C | TRP32 |
C | ARG33 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 103 |
Chain | Residue |
B | PHE12 |
B | GLY42 |
B | SCN103 |
C | ARG31 |
C | TRP32 |
C | ARG33 |
C | TRP34 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 104 |
Chain | Residue |
B | LEU19 |
B | PRO20 |
B | PRO21 |
C | PRO13 |
C | LYS14 |
C | GLU15 |
C | LYS16 |
Functional Information from PROSITE/UniProt
site_id | PS00459 |
Number of Residues | 38 |
Details | MYOTOXINS_1 Myotoxins signature. KqCHkKggHCfpKekiClppssdfgKmdCrwRwKCCKK |
Chain | Residue | Details |
A | LYS2-LYS39 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | SITE: Involved in the interaction surface toward Kv => ECO:0000305 |
Chain | Residue | Details |
A | SER23 | |
C | ASP24 | |
C | ARG33 | |
C | TRP34 | |
A | ASP24 | |
A | ARG33 | |
A | TRP34 | |
B | SER23 | |
B | ASP24 | |
B | ARG33 | |
B | TRP34 | |
C | SER23 |