EC Number   |
Cofactor |
Reference |
|---|
    1.3.3.4 | FAD |
- |
391015, 391016, 654950, 655018, 655341, 655497, 656991, 695527, 699636, 711307, 724557, 725177, 737734, 744734, 745140, 746296, 764083, 764914, 764954, 765503, 765577 |
| 1.3.3.4 | FAD |
1 molecule per subunit |
655194 |
| 1.3.3.4 | FAD |
a FAD molecule is non-covalently bound to domain I, binding structure, overview |
712895 |
| 1.3.3.4 | FAD |
ab initio quantum mechanics calculations are performed for FAD optimization at the HF/6-31+G level to determine the electrostatic potential by using the restrained electrostatic potential (RESP) method according to the Merz-Singh-Kollman scheme |
745134 |
| 1.3.3.4 | FAD |
analysis of the FAD binding region and binding structures using wild-type and mutant enzymes, detailed overview. Ser20 mutants can still bind FAD, but polarity in this position is favourable, yet not essential for the integrity of FAD binding. Glu39 mutants suggest that a negative charge at position 39 is clearly favoured for interaction with the ribose ring of FAD, as all non-conservative replacements can not bind sufficient FAD. Asp441 appears not to be directly involved in FAD binding but rather in stabilizing FAD, and polarity in this position appears important. Trp408 may play a role in orientating or stabilizing the bound substrate during catalysis, and a non-polar (or slightly polar) residue is favoured at this position. Aromaticity in this position appears not to be critical |
744202 |
| 1.3.3.4 | FAD |
binding structure analysis through molecular docking using the crystal structure of Nicotiana tabacum mitochondrial PPO enzyme, overview |
746243 |
| 1.3.3.4 | FAD |
enzyme interaction structure, overview |
726346 |
| 1.3.3.4 | FAD |
essential cofactor |
391002 |
| 1.3.3.4 | FAD |
modeling of binding structure, overview |
745787 |
| 1.3.3.4 | FAD |
no flavins detected |
390998 |
