6LPY
Crystal Structure of E447A Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C4CoA
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 | 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 | 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 | LEU445 |
A | TYR446 |
A | THR449 |
A | BUA702 |
A | COA703 |
A | HOH944 |
A | HOH953 |
A | HOH966 |
A | HOH989 |
A | HOH1028 |
A | LEU164 |
A | HOH1050 |
B | ARG326 |
B | GLN328 |
B | ILE345 |
B | HIS348 |
B | GLN420 |
B | THR421 |
B | GLY423 |
B | GLY424 |
B | HOH831 |
A | THR165 |
B | HOH907 |
A | GLY170 |
A | SER171 |
A | PHE196 |
A | ILE197 |
A | THR198 |
A | ILE442 |
site_id | AC2 |
Number of Residues | 30 |
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 | HOH849 |
A | HOH917 |
B | MET162 |
B | LEU164 |
B | THR165 |
B | GLY170 |
B | SER171 |
B | PHE196 |
B | THR198 |
B | ILE442 |
B | LEU445 |
B | TYR446 |
B | THR449 |
B | ALA451 |
B | BUA702 |
B | COA703 |
B | HOH927 |
B | HOH957 |
B | HOH959 |
B | HOH980 |
B | HOH1030 |
B | HOH1057 |
site_id | AC3 |
Number of Residues | 24 |
Details | binding site for residues BUA A 702 and COA A 703 |
Chain | Residue |
A | MET162 |
A | LEU164 |
A | SER171 |
A | VAL173 |
A | THR224 |
A | LYS225 |
A | ILE290 |
A | PHE294 |
A | GLU298 |
A | ARG301 |
A | TYR446 |
A | ALA447 |
A | GLY448 |
A | ILE452 |
A | ASP456 |
A | ARG460 |
A | LYS461 |
A | ARG464 |
A | FAD701 |
A | HOH876 |
A | HOH994 |
A | HOH1000 |
A | HOH1142 |
B | LYS338 |
site_id | AC4 |
Number of Residues | 28 |
Details | binding site for residues BUA B 702 and COA B 703 |
Chain | Residue |
B | ARG460 |
B | LYS461 |
B | FAD701 |
B | HOH807 |
B | HOH837 |
B | HOH842 |
B | HOH854 |
B | HOH866 |
B | HOH1038 |
B | HOH1088 |
B | HOH1122 |
B | HOH1135 |
B | HOH1196 |
A | LYS338 |
B | MET162 |
B | SER171 |
B | VAL173 |
B | THR224 |
B | ILE290 |
B | PHE294 |
B | GLU298 |
B | ARG301 |
B | MET303 |
B | TYR446 |
B | ALA447 |
B | GLY448 |
B | ILE452 |
B | ASP456 |
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 |