Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0009055 | molecular_function | electron transfer activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0009055 | molecular_function | electron transfer activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 399 |
| Chain | Residue |
| A | GLY200 |
| A | GLN243 |
| A | THR244 |
| A | GLY245 |
| A | GLY257 |
| A | ILE258 |
| A | SER259 |
| A | ALA261 |
| A | GLN263 |
| A | HIS264 |
| A | ASN278 |
| A | ARG201 |
| A | LYS279 |
| A | ASP280 |
| A | GLY295 |
| A | ASP296 |
| A | LEU297 |
| A | HOH608 |
| A | HOH614 |
| B | TYR13 |
| B | PHE38 |
| B | LEU182 |
| A | GLY202 |
| A | SER226 |
| A | ARG227 |
| A | ALA228 |
| A | GLN240 |
| A | VAL241 |
| A | GLY242 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP A 400 |
| Chain | Residue |
| B | PRO6 |
| B | VAL7 |
| B | ASN36 |
| B | ASP39 |
| B | ILE63 |
| B | ALA119 |
| B | GLY120 |
| B | GLN122 |
| B | ALA123 |
| B | ASN126 |
| B | MET128 |
| B | ASN129 |
| B | ALA130 |
| B | THR131 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD C 399 |
| Chain | Residue |
| B | HOH639 |
| C | GLY200 |
| C | ARG201 |
| C | GLY202 |
| C | SER226 |
| C | ARG227 |
| C | ALA228 |
| C | GLN240 |
| C | VAL241 |
| C | GLY242 |
| C | GLN243 |
| C | THR244 |
| C | GLY257 |
| C | ILE258 |
| C | SER259 |
| C | ALA261 |
| C | GLN263 |
| C | HIS264 |
| C | ASN278 |
| C | LYS279 |
| C | ASP280 |
| C | GLY295 |
| C | ASP296 |
| C | LEU297 |
| C | PHE298 |
| C | HOH609 |
| D | TYR13 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP C 400 |
| Chain | Residue |
| D | PRO6 |
| D | VAL7 |
| D | ASN36 |
| D | ASP39 |
| D | ILE63 |
| D | ALA119 |
| D | GLY120 |
| D | GLN122 |
| D | ALA123 |
| D | ASN126 |
| D | MET128 |
| D | ASN129 |
| D | ALA130 |
| D | THR131 |
| D | HOH606 |
Functional Information from PROSITE/UniProt
| site_id | PS00696 |
| Number of Residues | 27 |
| Details | ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYVAvGISGaIQHlaGmkdskvIvAIN |
| Chain | Residue | Details |
| A | LEU252-ASN278 | |
| site_id | PS01065 |
| Number of Residues | 21 |
| Details | ETF_BETA Electron transfer flavoprotein beta-subunit signature. VtRevDGGl.QtIavslPaVVT |
| Chain | Residue | Details |
| B | VAL159-THR179 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | TYR253 | |
| C | TYR253 | |
