1XTL
Crystal structure of P104H mutant of SOD-like protein from Bacillus subtilis.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043167 | molecular_function | ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016020 | cellular_component | membrane |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043167 | molecular_function | ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006801 | biological_process | superoxide metabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016020 | cellular_component | membrane |
| C | 0019430 | biological_process | removal of superoxide radicals |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043167 | molecular_function | ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006801 | biological_process | superoxide metabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016020 | cellular_component | membrane |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043167 | molecular_function | ion binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 1171 |
| Chain | Residue |
| B | HIS86 |
| B | TYR88 |
| B | HIS104 |
| B | HIS166 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1172 |
| Chain | Residue |
| B | HIS104 |
| B | HIS112 |
| B | HIS121 |
| B | ASP124 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 1173 |
| Chain | Residue |
| A | TYR88 |
| A | HIS104 |
| A | HIS166 |
| A | HIS86 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1174 |
| Chain | Residue |
| A | HIS104 |
| A | HIS112 |
| A | HIS121 |
| A | ASP124 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 1175 |
| Chain | Residue |
| C | HIS86 |
| C | TYR88 |
| C | HIS104 |
| C | HIS166 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 1176 |
| Chain | Residue |
| C | HIS104 |
| C | HIS112 |
| C | HIS121 |
| C | ASP124 |
| C | PRO176 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 1177 |
| Chain | Residue |
| D | HIS86 |
| D | TYR88 |
| D | HIS104 |
| D | HIS166 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 1178 |
| Chain | Residue |
| D | HIS104 |
| D | HIS112 |
| D | HIS121 |
| D | ASP124 |
| D | PRO176 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1326 |
| Chain | Residue |
| B | HIS71 |
| B | ASP137 |
| C | HIS71 |
| C | ASP137 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1327 |
| Chain | Residue |
| A | HIS71 |
| A | ASP137 |
| D | HIS71 |
| D | ASP137 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1328 |
| Chain | Residue |
| C | GLU89 |
| C | ASP157 |
| C | ASP159 |
| C | GLY160 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1329 |
| Chain | Residue |
| B | GLU89 |
| B | ASP157 |
| B | ASP159 |
| B | GLY160 |
| B | HOH1378 |
| B | HOH1396 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 1330 |
| Chain | Residue |
| D | GLU89 |
| D | ASP157 |
| D | ASP159 |
| D | GLY160 |
| D | HOH1392 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1331 |
| Chain | Residue |
| A | GLU89 |
| A | ASP157 |
| A | ASP159 |
| A | GLY160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | HIS71 | |
| B | ASP137 | |
| A | HIS71 | |
| A | ASP137 | |
| C | HIS71 | |
| C | ASP137 | |
| D | HIS71 | |
| D | ASP137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| B | HIS86 | |
| B | HIS166 | |
| A | HIS86 | |
| A | HIS166 | |
| C | HIS86 | |
| C | HIS166 | |
| D | HIS86 | |
| D | HIS166 |
