7DAY
Crystal structure of Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14), in TDP013-, and GSH-bound form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0004769 | molecular_function | steroid delta-isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0045456 | biological_process | ecdysteroid biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0004769 | molecular_function | steroid delta-isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042632 | biological_process | cholesterol homeostasis |
| B | 0045456 | biological_process | ecdysteroid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue H1X A 301 |
| Chain | Residue |
| A | PRO15 |
| A | LEU38 |
| A | PHE39 |
| A | GLN43 |
| A | SER114 |
| A | MET117 |
| A | LEU208 |
| A | GSH302 |
| A | HOH467 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue GSH A 302 |
| Chain | Residue |
| A | SER14 |
| A | LEU38 |
| A | GLN43 |
| A | HIS55 |
| A | SER56 |
| A | VAL57 |
| A | PRO58 |
| A | ASP69 |
| A | SER70 |
| A | HIS71 |
| A | PHE110 |
| A | H1X301 |
| A | HOH417 |
| A | HOH458 |
| A | HOH467 |
| A | HOH479 |
| A | HOH519 |
| A | HOH541 |
| A | HOH559 |
| B | SER107 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue H1X B 501 |
| Chain | Residue |
| A | GLU79 |
| A | TRP88 |
| A | ARG95 |
| B | GLU79 |
| B | TRP88 |
| B | ARG95 |
| B | MET96 |
| B | HOH615 |
| B | HOH680 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue H1X B 502 |
| Chain | Residue |
| B | PRO15 |
| B | LEU38 |
| B | PHE39 |
| B | PHE110 |
| B | ASP113 |
| B | SER114 |
| B | LEU208 |
| B | GSH503 |
| B | HOH631 |
| B | HOH633 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue GSH B 503 |
| Chain | Residue |
| A | SER107 |
| B | SER14 |
| B | PRO16 |
| B | GLN43 |
| B | HIS55 |
| B | SER56 |
| B | VAL57 |
| B | PRO58 |
| B | ASP69 |
| B | SER70 |
| B | HIS71 |
| B | PHE110 |
| B | H1X502 |
| B | HOH607 |
| B | HOH633 |
| B | HOH661 |
| B | HOH672 |
| B | HOH690 |
| B | HOH747 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue DTT B 504 |
| Chain | Residue |
| B | LEU26 |
| B | LEU87 |
| B | LEU159 |
| B | GLN181 |
| B | HOH642 |
| B | HOH795 |
