4PW3
Crystal structure of the sulfite dehydrogenase SorT from Sinorhizobium meliloti
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0008482 | molecular_function | sulfite oxidase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0008482 | molecular_function | sulfite oxidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0030151 | molecular_function | molybdenum ion binding |
| B | 0043546 | molecular_function | molybdopterin cofactor binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0006790 | biological_process | sulfur compound metabolic process |
| C | 0008482 | molecular_function | sulfite oxidase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0030151 | molecular_function | molybdenum ion binding |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006790 | biological_process | sulfur compound metabolic process |
| D | 0008482 | molecular_function | sulfite oxidase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0030151 | molecular_function | molybdenum ion binding |
| D | 0043546 | molecular_function | molybdopterin cofactor binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MSS A 401 |
| Chain | Residue |
| A | TYR76 |
| A | VAL201 |
| A | HIS228 |
| A | ARG233 |
| A | GLY241 |
| A | VAL242 |
| A | ASN244 |
| A | ILE245 |
| A | LYS246 |
| A | TYR267 |
| A | HOH602 |
| A | ILE77 |
| A | ARG78 |
| A | ASN79 |
| A | ASN80 |
| A | CYS127 |
| A | SER128 |
| A | GLY186 |
| A | GLU188 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MSS B 401 |
| Chain | Residue |
| B | TYR76 |
| B | ILE77 |
| B | ARG78 |
| B | ASN79 |
| B | ASN80 |
| B | LEU125 |
| B | CYS127 |
| B | SER128 |
| B | GLY186 |
| B | GLU188 |
| B | VAL201 |
| B | HIS228 |
| B | ARG233 |
| B | GLY241 |
| B | VAL242 |
| B | ASN244 |
| B | LYS246 |
| B | TYR247 |
| B | TYR267 |
| B | HOH585 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| A | ASN220 |
| A | ARG222 |
| B | PRO71 |
| B | GLU72 |
| B | ASN220 |
| B | ARG222 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MSS C 401 |
| Chain | Residue |
| C | TYR76 |
| C | ILE77 |
| C | ARG78 |
| C | ASN79 |
| C | ASN80 |
| C | LEU125 |
| C | CYS127 |
| C | SER128 |
| C | GLY186 |
| C | GLU188 |
| C | VAL201 |
| C | HIS228 |
| C | ARG233 |
| C | GLY241 |
| C | VAL242 |
| C | ASN244 |
| C | LYS246 |
| C | TYR247 |
| C | TYR267 |
| C | HOH603 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| C | GLU72 |
| C | ASN220 |
| C | ARG222 |
| D | GLU72 |
| D | ASN220 |
| D | ARG222 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MSS D 401 |
| Chain | Residue |
| D | TYR76 |
| D | ILE77 |
| D | ARG78 |
| D | ASN79 |
| D | ASN80 |
| D | LEU125 |
| D | CYS127 |
| D | SER128 |
| D | GLU188 |
| D | VAL201 |
| D | HIS228 |
| D | ARG233 |
| D | GLY241 |
| D | VAL242 |
| D | ASN244 |
| D | LYS246 |
| D | TYR247 |
| D | TYR267 |
| D | HOH586 |
