7DB0
Crystal structure of Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14), in dimedone-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 | 6 |
Details | binding site for residue DC1 A 301 |
Chain | Residue |
A | PRO15 |
A | PHE110 |
A | ASP113 |
A | SER114 |
A | THR172 |
A | HOH409 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue DMS A 302 |
Chain | Residue |
A | TYR147 |
A | ASN150 |
A | HOH441 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue DMS A 303 |
Chain | Residue |
A | ASP152 |
A | PHE153 |
A | ARG187 |
A | ALA191 |
A | HOH447 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue DMS A 304 |
Chain | Residue |
A | LEU27 |
A | PHE35 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue DMS A 305 |
Chain | Residue |
A | ASP28 |
A | ILE29 |
A | ASP30 |
A | PHE81 |
A | GLN210 |
A | SER214 |
A | HOH404 |
A | HOH411 |
A | HOH549 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue DMS A 306 |
Chain | Residue |
A | TYR10 |
A | GLU12 |
A | LEU33 |
A | HOH633 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue DMS A 307 |
Chain | Residue |
A | HIS62 |
A | LEU65 |
A | HIS76 |
A | LYS80 |
A | HOH416 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue DMS A 308 |
Chain | Residue |
A | SER107 |
A | ARG111 |
A | ARG112 |
A | HOH557 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue DMS A 309 |
Chain | Residue |
A | CYS106 |
A | PHE110 |
A | HOH528 |
A | HOH620 |
B | HOH453 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue DC1 B 301 |
Chain | Residue |
B | PRO15 |
B | PHE110 |
B | ASP113 |
B | SER114 |
B | THR172 |
B | HOH445 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue DMS B 302 |
Chain | Residue |
B | GLN181 |
B | HOH478 |
B | HOH555 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue DMS B 303 |
Chain | Residue |
A | HOH628 |
B | GLU12 |
B | LEU33 |
B | HOH406 |
B | HOH626 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue DMS B 304 |
Chain | Residue |
A | HIS92 |
B | HIS62 |
B | LEU65 |
B | HIS76 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue DMS B 305 |
Chain | Residue |
B | SER56 |
B | VAL57 |
B | PRO58 |
B | THR68 |
B | ASP69 |
B | SER70 |
B | HOH420 |