6KSB
Crystal Structure of E447A M130G Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C16CoA
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 | 7 |
| Details | binding site for residue GOL A 701 |
| Chain | Residue |
| A | SER2 |
| A | HIS3 |
| A | ALA54 |
| A | GLU55 |
| A | PHE57 |
| A | VAL58 |
| A | HOH869 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 702 |
| Chain | Residue |
| A | THR165 |
| A | GLY170 |
| A | SER171 |
| A | PHE196 |
| A | ILE197 |
| A | THR198 |
| A | ILE442 |
| A | LEU445 |
| A | TYR446 |
| A | ALA447 |
| A | THR449 |
| A | GLN455 |
| A | PLM703 |
| A | COA704 |
| A | HOH899 |
| A | HOH905 |
| A | HOH933 |
| A | HOH958 |
| A | HOH962 |
| B | ARG326 |
| B | GLN328 |
| B | ILE345 |
| B | HIS348 |
| B | GLN420 |
| B | THR421 |
| B | GLY423 |
| B | GLY424 |
| B | HOH889 |
| B | HOH892 |
| B | HOH894 |
| A | MET162 |
| A | LEU164 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 701 |
| Chain | Residue |
| B | SER2 |
| B | HIS3 |
| B | ALA54 |
| B | GLU55 |
| B | PHE57 |
| B | VAL58 |
| B | HOH858 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | binding site for residue FAD B 702 |
| Chain | Residue |
| A | ARG326 |
| A | GLN328 |
| A | ILE345 |
| A | HIS348 |
| A | GLN420 |
| A | THR421 |
| A | GLY423 |
| A | GLY424 |
| A | HOH847 |
| A | HOH868 |
| B | MET162 |
| B | LEU164 |
| B | THR165 |
| B | GLY170 |
| B | SER171 |
| B | PHE196 |
| B | ILE197 |
| B | THR198 |
| B | ILE442 |
| B | LEU445 |
| B | TYR446 |
| B | THR449 |
| B | GLN455 |
| B | PLM703 |
| B | COA704 |
| B | HOH843 |
| B | HOH904 |
| B | HOH948 |
| B | HOH951 |
| B | HOH975 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residues PLM A 703 and COA A 704 |
| Chain | Residue |
| A | HOH844 |
| A | HOH864 |
| A | HOH886 |
| A | HOH918 |
| A | HOH928 |
| A | HOH972 |
| A | HOH1026 |
| B | LYS338 |
| A | TYR126 |
| A | MET127 |
| A | SER171 |
| A | VAL173 |
| A | THR224 |
| A | LYS225 |
| A | ILE290 |
| A | PHE294 |
| A | GLU298 |
| A | GLN299 |
| A | ARG301 |
| A | TYR446 |
| A | ALA447 |
| A | GLY448 |
| A | ILE452 |
| A | ASP456 |
| A | ARG460 |
| A | LYS461 |
| A | ARG464 |
| A | FAD702 |
| A | HOH806 |
| A | HOH807 |
| A | HOH816 |
| site_id | AC6 |
| Number of Residues | 35 |
| Details | binding site for residues PLM B 703 and COA B 704 |
| Chain | Residue |
| A | LYS338 |
| B | TYR126 |
| B | MET127 |
| B | MET134 |
| B | SER171 |
| B | VAL173 |
| B | THR198 |
| B | THR224 |
| B | LYS225 |
| B | ILE290 |
| B | PHE294 |
| B | GLU298 |
| B | ALA300 |
| B | ARG301 |
| B | TYR446 |
| B | ALA447 |
| B | GLY448 |
| B | ILE452 |
| B | ASP456 |
| B | ARG460 |
| B | LYS461 |
| B | ARG464 |
| B | FAD702 |
| B | HOH810 |
| B | HOH814 |
| B | HOH815 |
| B | HOH825 |
| B | HOH845 |
| B | HOH872 |
| B | HOH896 |
| B | HOH898 |
| B | HOH920 |
| B | HOH954 |
| B | HOH993 |
| B | HOH1039 |
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 | ALA447 | |
| B | ALA447 |
| 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 | ALA447 | |
| B | THR449 | |
| B | ASP456 | |
| B | ARG460 | |
| A | THR198 | |
| A | THR224 | |
| A | ARG301 | |
| A | ARG326 | |
| A | LYS338 | |
| A | GLN420 | |
| A | ALA447 |
