5IDU
Crystal structure of an acyl-CoA dehydrogenase domain protein from Burkholderia phymatum bound to FAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | PHE135 |
| A | GLU377 |
| A | VAL378 |
| A | EDO504 |
| A | HOH657 |
| A | HOH673 |
| A | HOH682 |
| A | HOH705 |
| A | HOH722 |
| A | HOH742 |
| A | HOH813 |
| A | LEU137 |
| B | ARG278 |
| B | MET280 |
| B | LEU285 |
| B | PHE288 |
| B | GLN346 |
| B | LEU347 |
| B | GLY349 |
| B | GLY350 |
| B | VAL353 |
| B | HOH616 |
| A | SER138 |
| B | HOH710 |
| B | HOH745 |
| D | GLN289 |
| A | GLY143 |
| A | SER144 |
| A | TRP168 |
| A | SER170 |
| A | HIS217 |
| A | TYR372 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ALA11 |
| A | LEU84 |
| A | GLU87 |
| A | LEU261 |
| A | ARG265 |
| A | TYR310 |
| A | HOH749 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | ARG265 |
| A | ASP303 |
| A | HOH630 |
| A | HOH680 |
| D | ARG324 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | TYR372 |
| A | GLU373 |
| A | FAD501 |
| A | HOH796 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| A | ARG278 |
| A | MET280 |
| A | LEU285 |
| A | PHE288 |
| A | GLN346 |
| A | LEU347 |
| A | GLY349 |
| A | GLY350 |
| A | VAL353 |
| A | HOH604 |
| A | HOH607 |
| A | HOH691 |
| A | HOH771 |
| B | PHE135 |
| B | LEU137 |
| B | SER138 |
| B | GLY143 |
| B | SER144 |
| B | TRP168 |
| B | SER170 |
| B | HIS217 |
| B | TYR372 |
| B | GLU377 |
| B | VAL378 |
| B | EDO504 |
| B | HOH650 |
| B | HOH652 |
| B | HOH706 |
| B | HOH714 |
| B | HOH731 |
| B | HOH785 |
| C | GLN289 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | ALA11 |
| B | LEU84 |
| B | GLU87 |
| B | LEU261 |
| B | ARG265 |
| B | TYR310 |
| B | HOH704 |
| B | HOH822 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | ARG265 |
| B | ASP303 |
| B | HOH622 |
| B | HOH695 |
| C | ARG324 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | TYR372 |
| B | GLU373 |
| B | FAD501 |
| B | HOH751 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | LEU137 |
| C | SER138 |
| C | GLY143 |
| C | SER144 |
| C | TRP168 |
| C | SER170 |
| C | HIS217 |
| C | ALA368 |
| C | TYR372 |
| C | ALA375 |
| C | GLU377 |
| C | HOH625 |
| C | HOH654 |
| C | HOH686 |
| C | HOH709 |
| C | HOH724 |
| C | HOH731 |
| C | HOH762 |
| C | HOH770 |
| D | ARG278 |
| D | MET280 |
| D | LEU285 |
| D | GLN346 |
| D | LEU347 |
| D | GLY349 |
| D | GLY350 |
| D | HOH604 |
| D | HOH606 |
| D | HOH622 |
| B | GLN289 |
| C | PHE135 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | ALA11 |
| C | LEU84 |
| C | GLU87 |
| C | LEU261 |
| C | ARG265 |
| C | TYR310 |
| C | HOH659 |
| C | HOH725 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| B | ARG324 |
| C | ARG265 |
| C | ASP303 |
| C | HOH618 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | ARG86 |
| C | LEU105 |
| C | PHE252 |
| C | GLU373 |
| site_id | AD4 |
| Number of Residues | 32 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| A | GLN289 |
| C | ARG278 |
| C | MET280 |
| C | LEU285 |
| C | PHE288 |
| C | GLN346 |
| C | LEU347 |
| C | GLY349 |
| C | GLY350 |
| C | VAL353 |
| C | HOH613 |
| C | HOH675 |
| C | HOH739 |
| D | PHE135 |
| D | LEU137 |
| D | SER138 |
| D | GLY143 |
| D | SER144 |
| D | TRP168 |
| D | SER170 |
| D | HIS217 |
| D | TYR372 |
| D | ALA375 |
| D | GLU377 |
| D | HOH640 |
| D | HOH645 |
| D | HOH648 |
| D | HOH657 |
| D | HOH688 |
| D | HOH705 |
| D | HOH716 |
| D | HOH777 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | ALA11 |
| D | LEU84 |
| D | GLU87 |
| D | LEU261 |
| D | ARG265 |
| D | TYR310 |
| D | HOH697 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| A | ARG324 |
| A | LEU387 |
| D | ARG265 |
| D | ALA299 |
| D | ILE302 |
| D | ASP303 |
| D | HOH615 |
| D | HOH775 |
Functional Information from PROSITE/UniProt
| site_id | PS00072 |
| Number of Residues | 13 |
| Details | ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. ALSEpdAGSDvaA |
| Chain | Residue | Details |
| A | ALA136-ALA148 |
