3SZS
Crystal structure analysis of hellethionin D
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006952 | biological_process | defense response |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| A | 0050832 | biological_process | defense response to fungus |
| A | 0090729 | molecular_function | toxin activity |
| B | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006952 | biological_process | defense response |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0050832 | biological_process | defense response to fungus |
| B | 0090729 | molecular_function | toxin activity |
| C | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006952 | biological_process | defense response |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0050832 | biological_process | defense response to fungus |
| C | 0090729 | molecular_function | toxin activity |
| D | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006952 | biological_process | defense response |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0050832 | biological_process | defense response to fungus |
| D | 0090729 | molecular_function | toxin activity |
| E | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| E | 0005576 | cellular_component | extracellular region |
| E | 0006952 | biological_process | defense response |
| E | 0035821 | biological_process | modulation of process of another organism |
| E | 0050830 | biological_process | defense response to Gram-positive bacterium |
| E | 0050832 | biological_process | defense response to fungus |
| E | 0090729 | molecular_function | toxin activity |
| F | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| F | 0005576 | cellular_component | extracellular region |
| F | 0006952 | biological_process | defense response |
| F | 0035821 | biological_process | modulation of process of another organism |
| F | 0050830 | biological_process | defense response to Gram-positive bacterium |
| F | 0050832 | biological_process | defense response to fungus |
| F | 0090729 | molecular_function | toxin activity |
| G | 0001897 | biological_process | symbiont-mediated cytolysis of host cell |
| G | 0005576 | cellular_component | extracellular region |
| G | 0006952 | biological_process | defense response |
| G | 0035821 | biological_process | modulation of process of another organism |
| G | 0050830 | biological_process | defense response to Gram-positive bacterium |
| G | 0050832 | biological_process | defense response to fungus |
| G | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 50 |
| Chain | Residue |
| A | SER22 |
| A | THR25 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 51 |
| Chain | Residue |
| A | GLN23 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 52 |
| Chain | Residue |
| A | THR25 |
| E | ASN11 |
| E | ASN14 |
| E | HOH102 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 53 |
| Chain | Residue |
| E | HOH102 |
| E | HOH131 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 54 |
| Chain | Residue |
| A | ARG17 |
| A | GLY20 |
| A | GLY21 |
| A | HOH106 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 55 |
| Chain | Residue |
| A | HIS34 |
| A | HOH103 |
| A | HOH126 |
| F | THR25 |
| F | CL57 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 50 |
| Chain | Residue |
| B | THR39 |
| B | CYS40 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 51 |
| Chain | Residue |
| B | THR39 |
| B | HOH121 |
| D | THR38 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 50 |
| Chain | Residue |
| C | GLY20 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 51 |
| Chain | Residue |
| C | THR38 |
| E | CYS12 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 50 |
| Chain | Residue |
| D | THR39 |
| D | CYS40 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 51 |
| Chain | Residue |
| D | THR36 |
| D | HOH151 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA D 52 |
| Chain | Residue |
| D | SER42 |
| D | SER42 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 53 |
| Chain | Residue |
| D | ARG5 |
| D | ARG5 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E 50 |
| Chain | Residue |
| B | ARG10 |
| B | ASN14 |
| E | SER22 |
| E | THR25 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 51 |
| Chain | Residue |
| B | THR7 |
| E | THR36 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 52 |
| Chain | Residue |
| E | ARG17 |
| E | GLY20 |
| E | GLY21 |
| E | HOH111 |
| G | LYS1 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E 53 |
| Chain | Residue |
| E | GLN23 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA E 54 |
| Chain | Residue |
| E | ASN6 |
| E | HOH157 |
| F | SER43 |
| F | HOH135 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 55 |
| Chain | Residue |
| E | THR39 |
| E | CYS40 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA E 56 |
| Chain | Residue |
| E | ARG10 |
| E | ASN14 |
| G | HOH104 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA E 57 |
| Chain | Residue |
| E | THR37 |
| E | HOH142 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 58 |
| Chain | Residue |
| E | SER42 |
| E | SER43 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA E 59 |
| Chain | Residue |
| B | ASN6 |
| E | HOH123 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL E 60 |
| Chain | Residue |
| E | GLY27 |
| E | CYS32 |
| E | ILE33 |
| E | CL62 |
| E | CL63 |
| E | HOH112 |
| E | HOH114 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL E 61 |
| Chain | Residue |
| E | PRO24 |
| E | GLY27 |
| E | ILE28 |
| E | CL62 |
| E | HOH146 |
| E | HOH153 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL E 62 |
| Chain | Residue |
| E | CL60 |
| E | CL61 |
| E | CL66 |
| E | HOH113 |
| E | HOH113 |
| E | HOH115 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL E 63 |
| Chain | Residue |
| E | ASP31 |
| E | ILE33 |
| E | HIS44 |
| E | CL60 |
| E | HOH114 |
| E | HOH115 |
| site_id | DC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL E 64 |
| Chain | Residue |
| E | ASN6 |
| E | THR7 |
| E | CL65 |
| E | HOH118 |
| E | HOH119 |
| F | ILE33 |
| F | HIS34 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL E 65 |
| Chain | Residue |
| E | ARG5 |
| E | ASN6 |
| E | SER46 |
| E | CL64 |
| E | HOH119 |
| E | HOH157 |
| site_id | DC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL E 66 |
| Chain | Residue |
| E | ILE28 |
| E | ILE33 |
| E | HIS34 |
| E | CL62 |
| E | HOH113 |
| E | HOH146 |
| E | HOH153 |
| site_id | DC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL F 50 |
| Chain | Residue |
| C | ASN6 |
| F | ARG5 |
| F | ASN6 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA F 51 |
| Chain | Residue |
| E | THR7 |
| E | HOH154 |
| F | CYS32 |
| F | ILE33 |
| F | HIS34 |
| site_id | DC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL F 52 |
| Chain | Residue |
| F | ASN6 |
| F | THR7 |
| F | LEU8 |
| F | HOH146 |
| site_id | DC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA F 53 |
| Chain | Residue |
| F | THR36 |
| site_id | DC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL F 54 |
| Chain | Residue |
| E | HOH150 |
| F | PRO41 |
| F | SER42 |
| F | SER43 |
| site_id | EC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL F 55 |
| Chain | Residue |
| F | THR37 |
| F | THR38 |
| site_id | EC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 56 |
| Chain | Residue |
| F | ASN11 |
| F | HOH101 |
| F | HOH138 |
| G | CYS12 |
| site_id | EC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL F 57 |
| Chain | Residue |
| A | HIS34 |
| A | CL55 |
| A | HOH102 |
| A | HOH103 |
| A | HOH115 |
| F | SER22 |
| F | PRO24 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA G 50 |
| Chain | Residue |
| B | HOH150 |
| B | HOH151 |
| D | ASN11 |
| G | HOH103 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL G 51 |
| Chain | Residue |
| G | GLY21 |
| G | SER22 |
| G | THR25 |
| G | HOH140 |
| site_id | EC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL G 52 |
| Chain | Residue |
| G | THR38 |
| G | THR39 |
| site_id | EC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA G 53 |
| Chain | Residue |
| A | HOH121 |
| G | GLY27 |
| G | CYS32 |
| G | CL62 |
| G | HOH123 |
| site_id | EC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA G 54 |
| Chain | Residue |
| B | ARG17 |
| G | ARG17 |
| G | HOH110 |
| site_id | EC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL G 55 |
| Chain | Residue |
| G | SER2 |
| site_id | FC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL G 56 |
| Chain | Residue |
| G | THR39 |
| G | CYS40 |
| G | HOH145 |
| site_id | FC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL G 57 |
| Chain | Residue |
| G | VAL35 |
| G | THR36 |
| G | HOH122 |
| site_id | FC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA G 58 |
| Chain | Residue |
| G | THR39 |
| G | CYS40 |
| site_id | FC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL G 59 |
| Chain | Residue |
| G | SER42 |
| G | SER43 |
| site_id | FC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA G 60 |
| Chain | Residue |
| F | SER46 |
| F | HOH138 |
| G | LEU8 |
| G | HOH121 |
| G | HOH151 |
| site_id | FC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA G 61 |
| Chain | Residue |
| A | HOH119 |
| C | HOH136 |
| G | SER22 |
| site_id | FC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL G 62 |
| Chain | Residue |
| F | HOH129 |
| G | GLY27 |
| G | ILE28 |
| G | ASP31 |
| G | NA53 |
Functional Information from PROSITE/UniProt
| site_id | PS00271 |
| Number of Residues | 14 |
| Details | THIONIN Plant thionins signature. CCrntlaRncYnaC |
| Chain | Residue | Details |
| A | CYS3-CYS16 |
