5JSC
Crystal structure of a Putative acyl-CoA dehydrogenase from Burkholderia xenovorans
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 | 29 |
| Details | binding site for residue FAD A 500 |
| Chain | Residue |
| A | PHE136 |
| A | HOH657 |
| A | HOH661 |
| A | HOH674 |
| A | HOH682 |
| A | HOH705 |
| A | HOH764 |
| A | HOH809 |
| B | ARG279 |
| B | MET281 |
| B | LEU286 |
| A | LEU138 |
| B | PHE289 |
| B | GLN347 |
| B | LEU348 |
| B | GLY350 |
| B | GLY351 |
| B | VAL354 |
| B | HOH620 |
| B | HOH690 |
| B | HOH726 |
| D | GLN290 |
| A | SER139 |
| A | GLY144 |
| A | SER145 |
| A | TRP169 |
| A | SER171 |
| A | TYR373 |
| A | GLU378 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | ARG21 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ALA12 |
| A | LEU85 |
| A | GLU88 |
| A | LEU262 |
| A | ARG266 |
| A | TYR311 |
| A | HOH766 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue FAD B 500 |
| Chain | Residue |
| A | ARG279 |
| A | MET281 |
| A | LEU286 |
| A | PHE289 |
| A | GLN347 |
| A | LEU348 |
| A | GLY350 |
| A | GLY351 |
| A | VAL354 |
| A | HOH622 |
| A | HOH677 |
| A | HOH714 |
| B | PHE136 |
| B | LEU138 |
| B | SER139 |
| B | GLY144 |
| B | SER145 |
| B | TRP169 |
| B | SER171 |
| B | TYR373 |
| B | GLU378 |
| B | VAL379 |
| B | HOH654 |
| B | HOH675 |
| B | HOH703 |
| B | HOH712 |
| B | HOH736 |
| B | HOH784 |
| B | HOH805 |
| B | HOH853 |
| B | HOH871 |
| C | GLN290 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 501 |
| Chain | Residue |
| B | ARG21 |
| B | HOH924 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | ALA12 |
| B | GLU88 |
| B | LEU262 |
| B | ARG266 |
| B | ALA307 |
| B | TYR311 |
| B | HOH783 |
| B | HOH916 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | GLY205 |
| B | GLU207 |
| D | ARG222 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | GLU19 |
| B | ARG21 |
| B | ARG81 |
| B | HOH608 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | HOH699 |
| C | HOH704 |
| C | HOH742 |
| C | HOH749 |
| C | HOH819 |
| C | HOH831 |
| C | HOH898 |
| D | ARG279 |
| D | MET281 |
| D | PHE282 |
| D | LEU286 |
| D | PHE289 |
| D | GLN347 |
| D | LEU348 |
| D | GLY350 |
| D | GLY351 |
| D | VAL354 |
| D | HOH642 |
| D | HOH760 |
| B | GLN290 |
| C | PHE136 |
| C | LEU138 |
| C | SER139 |
| C | GLY144 |
| C | SER145 |
| C | TRP169 |
| C | ILE170 |
| C | SER171 |
| C | ILE372 |
| C | TYR373 |
| C | ALA376 |
| C | GLU378 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | ARG21 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| C | ALA12 |
| C | LEU85 |
| C | GLU88 |
| C | LEU262 |
| C | ARG266 |
| C | TYR311 |
| C | HOH886 |
| C | HOH921 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| B | HIS333 |
| C | GLN298 |
| C | LEU301 |
| C | THR302 |
| C | SER305 |
| C | HIS333 |
| C | HOH647 |
| C | HOH690 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 505 |
| Chain | Residue |
| C | GLU19 |
| C | ARG81 |
| C | GLN319 |
| C | HOH627 |
| C | HOH772 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 C 506 |
| Chain | Residue |
| C | THR77 |
| C | ILE78 |
| C | ARG317 |
| C | HOH601 |
| C | HOH614 |
| C | HOH618 |
| C | HOH629 |
| C | HOH830 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 507 |
| Chain | Residue |
| C | SER94 |
| C | GLY95 |
| C | LEU96 |
| C | HOH615 |
| C | HOH652 |
| C | HOH723 |
| site_id | AD7 |
| Number of Residues | 34 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| A | GLN290 |
| C | ARG279 |
| C | MET281 |
| C | PHE282 |
| C | LEU286 |
| C | PHE289 |
| C | GLN347 |
| C | LEU348 |
| C | GLY350 |
| C | GLY351 |
| C | VAL354 |
| C | HOH606 |
| C | HOH660 |
| C | HOH700 |
| D | PHE136 |
| D | LEU138 |
| D | SER139 |
| D | GLY144 |
| D | SER145 |
| D | TRP169 |
| D | ILE170 |
| D | SER171 |
| D | ILE372 |
| D | TYR373 |
| D | ALA376 |
| D | GLU378 |
| D | HOH665 |
| D | HOH673 |
| D | HOH696 |
| D | HOH720 |
| D | HOH789 |
| D | HOH791 |
| D | HOH837 |
| D | HOH883 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 502 |
| Chain | Residue |
| D | ARG21 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | ALA12 |
| D | LEU85 |
| D | GLU88 |
| D | LEU262 |
| D | ARG266 |
| D | TYR311 |
| D | HOH655 |
| D | HOH853 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 D 504 |
| Chain | Residue |
| A | HIS333 |
| D | GLN298 |
| D | LEU301 |
| D | THR302 |
| D | SER305 |
| D | HIS333 |
| D | HOH631 |
| D | HOH682 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 505 |
| Chain | Residue |
| D | THR77 |
| D | ILE78 |
| D | ARG317 |
| D | HOH604 |
| D | HOH611 |
| D | HOH808 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 506 |
| Chain | Residue |
| D | GLU19 |
| D | ARG81 |
| D | GLN319 |
| D | HOH705 |
Functional Information from PROSITE/UniProt
| site_id | PS00072 |
| Number of Residues | 13 |
| Details | ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. ALSEpeAGSDvaA |
| Chain | Residue | Details |
| A | ALA137-ALA149 |
