4M05
Crystal Structure of Mutant Chlorite Dismutase from Candidatus Nitrospira defluvii R173E
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050587 | molecular_function | chlorite O2-lyase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050587 | molecular_function | chlorite O2-lyase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050587 | molecular_function | chlorite O2-lyase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050587 | molecular_function | chlorite O2-lyase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050587 | molecular_function | chlorite O2-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 301 |
| Chain | Residue |
| A | PRO108 |
| A | ALA164 |
| A | PHE186 |
| A | THR188 |
| A | PHE190 |
| A | LEU201 |
| A | LEU205 |
| A | PHE217 |
| A | THR109 |
| A | TYR110 |
| A | VAL111 |
| A | ILE139 |
| A | LYS141 |
| A | TRP145 |
| A | HIS160 |
| A | THR161 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 301 |
| Chain | Residue |
| B | PRO108 |
| B | THR109 |
| B | TYR110 |
| B | VAL111 |
| B | ILE139 |
| B | LYS141 |
| B | TRP145 |
| B | MET157 |
| B | HIS160 |
| B | THR161 |
| B | ALA164 |
| B | PHE186 |
| B | PHE190 |
| B | LEU201 |
| B | LEU205 |
| B | GLU210 |
| B | PHE217 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | LYS140 |
| B | ARG216 |
| B | HOH406 |
| D | HIS219 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 301 |
| Chain | Residue |
| C | PRO108 |
| C | THR109 |
| C | TYR110 |
| C | VAL111 |
| C | LEU122 |
| C | ILE139 |
| C | LYS141 |
| C | TRP145 |
| C | MET157 |
| C | HIS160 |
| C | THR161 |
| C | ALA164 |
| C | LEU168 |
| C | PHE186 |
| C | PHE190 |
| C | LEU205 |
| C | PHE217 |
| C | HOH414 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | GLU39 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM D 301 |
| Chain | Residue |
| D | PRO108 |
| D | THR109 |
| D | TYR110 |
| D | VAL111 |
| D | ILE139 |
| D | LYS141 |
| D | MET157 |
| D | HIS160 |
| D | THR161 |
| D | ALA164 |
| D | PHE186 |
| D | PHE190 |
| D | LEU201 |
| D | LEU205 |
| D | PHE217 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 302 |
| Chain | Residue |
| D | LYS140 |
| D | ARG216 |
| E | HIS219 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM E 301 |
| Chain | Residue |
| E | PRO108 |
| E | THR109 |
| E | TYR110 |
| E | ILE139 |
| E | LYS141 |
| E | TRP145 |
| E | MET157 |
| E | HIS160 |
| E | THR161 |
| E | ALA164 |
| E | LEU168 |
| E | PHE186 |
| E | THR188 |
| E | PHE190 |
| E | LEU205 |
| E | PHE217 |
