5VE4
Crystal structure of persulfide dioxygenase-rhodanese fusion protein with rhodanese domain inactivating mutation (C314S) from Burkholderia phytofirmans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050313 | molecular_function | sulfur dioxygenase activity |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0070813 | biological_process | hydrogen sulfide metabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050313 | molecular_function | sulfur dioxygenase activity |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0070813 | biological_process | hydrogen sulfide metabolic process |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050313 | molecular_function | sulfur dioxygenase activity |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0070813 | biological_process | hydrogen sulfide metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS58 |
| A | HIS114 |
| A | ASP133 |
| A | HOH504 |
| A | HOH506 |
| A | HOH515 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | ALA316 |
| A | GLY318 |
| A | ARG319 |
| A | LEU198 |
| A | ASP202 |
| A | SER314 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 403 |
| Chain | Residue |
| A | GLN6 |
| A | GLN6 |
| A | TYR171 |
| A | TYR171 |
| A | THR180 |
| A | VAL181 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | HIS95 |
| A | ARG109 |
| B | GLU200 |
| B | GLU201 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS58 |
| B | HIS114 |
| B | ASP133 |
| B | HOH501 |
| B | HOH506 |
| B | HOH533 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | SER314 |
| B | ARG315 |
| B | ALA316 |
| B | GLY317 |
| B | GLY318 |
| B | ARG319 |
| C | LEU198 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue IMD B 403 |
| Chain | Residue |
| B | PHE8 |
| B | TYR15 |
| C | PHE8 |
| C | TYR15 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS58 |
| C | HIS114 |
| C | ASP133 |
| C | HOH501 |
| C | HOH503 |
| C | HOH514 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| B | LEU198 |
| B | ASP202 |
| C | SER314 |
| C | ARG315 |
| C | ALA316 |
| C | GLY317 |
| C | GLY318 |
| C | ARG319 |
