6LQ7
Crystal Structure of E447A Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C17CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004466 | molecular_function | long-chain fatty acyl-CoA dehydrogenase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| 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 | 30 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | MET162 |
| A | TYR446 |
| A | ALA447 |
| A | THR449 |
| A | X90702 |
| A | COA703 |
| A | HOH957 |
| A | HOH970 |
| A | HOH995 |
| A | HOH1026 |
| A | HOH1052 |
| A | LEU164 |
| A | HOH1069 |
| B | ARG326 |
| B | GLN328 |
| B | ILE345 |
| B | HIS348 |
| B | GLN420 |
| B | THR421 |
| B | GLY423 |
| B | GLY424 |
| B | HOH856 |
| A | THR165 |
| B | HOH880 |
| 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 | GLN420 |
| A | THR421 |
| A | GLY423 |
| A | GLY424 |
| A | HOH888 |
| A | HOH895 |
| A | HOH998 |
| B | MET162 |
| B | LEU164 |
| B | THR165 |
| B | GLY170 |
| B | SER171 |
| B | PHE196 |
| B | THR198 |
| B | ILE442 |
| B | LEU445 |
| B | TYR446 |
| B | ALA447 |
| B | THR449 |
| B | X90702 |
| B | COA703 |
| B | HOH903 |
| B | HOH948 |
| B | HOH994 |
| B | HOH1023 |
| B | HOH1051 |
| B | HOH1053 |
| site_id | AC3 |
| Number of Residues | 41 |
| Details | binding site for residues X90 A 702 and COA A 703 |
| Chain | Residue |
| A | HOH1189 |
| A | HOH1204 |
| B | LYS338 |
| A | TYR126 |
| A | MET130 |
| A | MET134 |
| A | ALA160 |
| A | MET162 |
| A | SER171 |
| A | VAL173 |
| A | THR224 |
| A | LYS225 |
| A | ILE290 |
| A | ALA291 |
| A | PHE294 |
| A | VAL296 |
| A | GLU298 |
| A | ARG301 |
| A | MET303 |
| A | TYR446 |
| A | ALA447 |
| A | GLY448 |
| A | ILE452 |
| A | ASP456 |
| A | ARG460 |
| A | LYS461 |
| A | ARG464 |
| A | FAD701 |
| A | HOH847 |
| A | HOH861 |
| A | HOH910 |
| A | HOH920 |
| A | HOH939 |
| A | HOH967 |
| A | HOH1012 |
| A | HOH1035 |
| A | HOH1041 |
| A | HOH1070 |
| A | HOH1083 |
| A | HOH1112 |
| A | HOH1138 |
| site_id | AC4 |
| Number of Residues | 38 |
| Details | binding site for residues X90 B 702 and COA B 703 |
| Chain | Residue |
| A | LYS338 |
| B | TYR126 |
| B | MET130 |
| B | ALA160 |
| B | MET162 |
| B | SER171 |
| B | VAL173 |
| B | THR224 |
| B | LYS225 |
| B | ILE290 |
| B | PHE294 |
| B | GLU298 |
| B | GLN299 |
| B | ARG301 |
| B | MET303 |
| B | TYR446 |
| B | ALA447 |
| B | GLY448 |
| B | ASP456 |
| B | ARG460 |
| B | LYS461 |
| B | ARG464 |
| B | FAD701 |
| B | HOH830 |
| B | HOH831 |
| B | HOH845 |
| B | HOH859 |
| B | HOH865 |
| B | HOH870 |
| B | HOH890 |
| B | HOH923 |
| B | HOH933 |
| B | HOH950 |
| B | HOH970 |
| B | HOH991 |
| B | HOH1030 |
| B | HOH1142 |
| B | HOH1222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"32601219","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32601219","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
