3LXT
Crystal structure of Glutathione S Transferase from Pseudomonas fluorescens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| A | 0016740 | molecular_function | transferase activity |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| B | 0016740 | molecular_function | transferase activity |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0006559 | biological_process | L-phenylalanine catabolic process |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| C | 0016740 | molecular_function | transferase activity |
| D | 0004364 | molecular_function | glutathione transferase activity |
| D | 0006559 | biological_process | L-phenylalanine catabolic process |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 3969 |
| Chain | Residue |
| A | GLU93 |
| A | LEU156 |
| A | GLY157 |
| A | GLN158 |
| A | ALA159 |
| A | GLY160 |
| A | HOH258 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 526 |
| Chain | Residue |
| A | TYR13 |
| A | SER65 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 528 |
| Chain | Residue |
| A | LEU145 |
| A | PRO149 |
| A | LEU150 |
| A | HOH218 |
| A | HOH229 |
| A | HOH859 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 3968 |
| Chain | Residue |
| B | GLU93 |
| B | LEU156 |
| B | GLY157 |
| B | ALA159 |
| B | GLY160 |
| B | HOH277 |
| B | HOH448 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 525 |
| Chain | Residue |
| B | LEU145 |
| B | PRO149 |
| B | LEU150 |
| B | HOH243 |
| B | HOH259 |
| B | HOH273 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 527 |
| Chain | Residue |
| B | TYR13 |
| B | PRO52 |
| B | SER65 |
| B | HOH944 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 523 |
| Chain | Residue |
| C | TYR13 |
| C | PRO52 |
| C | ASP64 |
| C | SER65 |
| C | HOH277 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 524 |
| Chain | Residue |
| C | LEU145 |
| C | LEU150 |
| C | HOH227 |
| C | HOH231 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 522 |
| Chain | Residue |
| D | SER65 |
| D | HOH1012 |
