6KPT
Crystal Structure of Acyl-CoA Dehydrogenase FadE5 from Mycobacteria smegmatis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004466 | molecular_function | long-chain fatty acyl-CoA dehydrogenase activity |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| A | 0070991 | molecular_function | medium-chain fatty acyl-CoA dehydrogenase activity |
| B | 0004466 | molecular_function | long-chain fatty acyl-CoA dehydrogenase activity |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| B | 0070991 | molecular_function | medium-chain fatty acyl-CoA dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | MET162 |
| A | GLU447 |
| A | THR449 |
| A | GLN455 |
| A | HOH886 |
| A | HOH892 |
| A | HOH925 |
| A | HOH1008 |
| A | HOH1022 |
| A | HOH1068 |
| B | ARG326 |
| A | LEU164 |
| B | GLN328 |
| B | ILE345 |
| B | HIS348 |
| B | GLN420 |
| B | THR421 |
| B | GLY424 |
| B | HOH834 |
| B | HOH940 |
| A | THR165 |
| A | GLY170 |
| A | SER171 |
| A | PHE196 |
| A | THR198 |
| A | ILE442 |
| A | LEU445 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| A | ARG326 |
| A | GLN328 |
| A | ILE345 |
| A | HIS348 |
| A | VAL351 |
| A | GLN420 |
| A | THR421 |
| A | GLY423 |
| A | GLY424 |
| A | HOH824 |
| A | HOH930 |
| B | MET162 |
| B | LEU164 |
| B | THR165 |
| B | GLY170 |
| B | SER171 |
| B | PHE196 |
| B | ILE197 |
| B | THR198 |
| B | ILE442 |
| B | LEU445 |
| B | TYR446 |
| B | GLU447 |
| B | THR449 |
| B | GLN455 |
| B | HOH896 |
| B | HOH919 |
| B | HOH982 |
| B | HOH1056 |
| B | HOH1112 |
| B | HOH1178 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:32601219 |
| Chain | Residue | Details |
| A | GLU447 | |
| B | GLU447 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32601219 |
| Chain | Residue | Details |
| A | MET162 | |
| A | THR449 | |
| A | ASP456 | |
| A | ARG460 | |
| B | MET162 | |
| B | SER171 | |
| B | THR198 | |
| B | THR224 | |
| B | ARG301 | |
| B | ARG326 | |
| B | LYS338 | |
| A | SER171 | |
| B | GLN420 | |
| B | GLU447 | |
| B | THR449 | |
| B | ASP456 | |
| B | ARG460 | |
| A | THR198 | |
| A | THR224 | |
| A | ARG301 | |
| A | ARG326 | |
| A | LYS338 | |
| A | GLN420 | |
| A | GLU447 |
