6NA6
Serial Femtosecond X-ray Crystallography Structure of ECR in complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003730 | molecular_function | mRNA 3'-UTR binding |
| A | 0003960 | molecular_function | NADPH:quinone reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043880 | molecular_function | crotonyl-CoA reductase activity |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003730 | molecular_function | mRNA 3'-UTR binding |
| B | 0003960 | molecular_function | NADPH:quinone reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0043880 | molecular_function | crotonyl-CoA reductase activity |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003730 | molecular_function | mRNA 3'-UTR binding |
| C | 0003960 | molecular_function | NADPH:quinone reductase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0043880 | molecular_function | crotonyl-CoA reductase activity |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003730 | molecular_function | mRNA 3'-UTR binding |
| D | 0003960 | molecular_function | NADPH:quinone reductase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0043880 | molecular_function | crotonyl-CoA reductase activity |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue NDP A 501 |
| Chain | Residue |
| A | TYR80 |
| A | LEU237 |
| A | VAL256 |
| A | SER257 |
| A | LYS261 |
| A | ARG276 |
| A | HIS317 |
| A | PRO318 |
| A | GLU321 |
| A | THR322 |
| A | CYS339 |
| A | TRP84 |
| A | ALA340 |
| A | THR342 |
| A | PHE366 |
| A | HOH617 |
| A | HOH627 |
| A | HOH629 |
| A | LEU205 |
| A | VAL206 |
| A | THR209 |
| A | TRP231 |
| A | GLY232 |
| A | GLY235 |
| A | GLY236 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue NDP B 501 |
| Chain | Residue |
| B | TYR80 |
| B | VAL206 |
| B | GLY232 |
| B | GLY235 |
| B | GLY236 |
| B | LEU237 |
| B | VAL256 |
| B | SER257 |
| B | LYS261 |
| B | ARG276 |
| B | HIS317 |
| B | PRO318 |
| B | GLU321 |
| B | THR322 |
| B | ALA340 |
| B | SER341 |
| B | THR342 |
| B | HOH613 |
| B | HOH635 |
| D | TRP355 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | binding site for residue NDP D 501 |
| Chain | Residue |
| B | TRP355 |
| D | TYR80 |
| D | LEU205 |
| D | THR209 |
| D | GLY232 |
| D | SER234 |
| D | GLY236 |
| D | LEU237 |
| D | VAL255 |
| D | VAL256 |
| D | SER257 |
| D | LYS261 |
| D | ARG276 |
| D | HIS317 |
| D | PRO318 |
| D | GLU321 |
| D | CYS339 |
| D | ALA340 |
| D | THR342 |
| D | HIS365 |
| D | PHE366 |
| D | ASN407 |
| D | HIS409 |
| D | HOH616 |
| D | HOH631 |
| D | HOH659 |
| D | HOH684 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue NDP C 501 |
| Chain | Residue |
| C | HOH681 |
| A | TRP355 |
| C | TYR80 |
| C | TRP84 |
| C | LEU205 |
| C | THR209 |
| C | GLY232 |
| C | GLY235 |
| C | GLY236 |
| C | LEU237 |
| C | VAL256 |
| C | SER257 |
| C | ARG276 |
| C | HIS317 |
| C | PRO318 |
| C | GLU321 |
| C | THR322 |
| C | CYS339 |
| C | ALA340 |
| C | THR342 |
| C | SER343 |
| C | HIS365 |
| C | PHE366 |
| C | ASN407 |
| C | GLN410 |
| C | HOH614 |
| C | HOH632 |
| C | HOH680 |
