3OM8
The crystal structure of a hydrolase from Pseudomonas aeruginosa PA01
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042952 | biological_process | beta-ketoadipate pathway |
| A | 0047570 | molecular_function | 3-oxoadipate enol-lactonase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042952 | biological_process | beta-ketoadipate pathway |
| B | 0047570 | molecular_function | 3-oxoadipate enol-lactonase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 265 |
| Chain | Residue |
| A | ASP195 |
| A | THR196 |
| A | ASP197 |
| A | LEU198 |
| A | GLN201 |
| A | HOH322 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 266 |
| Chain | Residue |
| A | LEU100 |
| A | SER33 |
| A | ILE34 |
| A | SER99 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MES B 265 |
| Chain | Residue |
| B | ASP195 |
| B | THR196 |
| B | ASP197 |
| B | LEU198 |
| B | GLN201 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 266 |
| Chain | Residue |
| B | SER33 |
| B | ILE34 |
| B | SER99 |
| B | LEU100 |
| B | LEU128 |
