4YSL
Crystal structure of SdoA from Pseudomonas putida in complex with glutathione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050313 | molecular_function | sulfur dioxygenase activity |
| A | 0070813 | biological_process | hydrogen sulfide metabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050313 | molecular_function | sulfur dioxygenase activity |
| B | 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 301 |
| Chain | Residue |
| A | HIS74 |
| A | HIS149 |
| A | ASP170 |
| A | GSH302 |
| A | HOH426 |
| A | HOH593 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue GSH A 302 |
| Chain | Residue |
| A | ALA180 |
| A | ARG181 |
| A | TYR214 |
| A | ARG250 |
| A | ARG253 |
| A | PRO260 |
| A | VAL261 |
| A | FE301 |
| A | HOH409 |
| A | HOH410 |
| A | HOH422 |
| A | HOH464 |
| A | HOH568 |
| A | HIS149 |
| A | ASP170 |
| A | TYR177 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue FE B 301 |
| Chain | Residue |
| B | HIS74 |
| B | HIS149 |
| B | ASP170 |
| B | GSH302 |
| B | HOH421 |
| B | HOH586 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue GSH B 302 |
| Chain | Residue |
| B | HIS149 |
| B | ASP170 |
| B | PHE173 |
| B | ALA180 |
| B | ARG181 |
| B | TYR214 |
| B | ARG250 |
| B | PRO260 |
| B | VAL261 |
| B | FE301 |
| B | HOH431 |
| B | HOH444 |
| B | HOH474 |
| B | HOH545 |
| B | HOH586 |
