6KRI
Crystal Structure of Acyl-CoA Dehydrogenase FadE5 from Mycobacteria smegmatis with product released
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 | TYR446 |
| A | GLU447 |
| A | THR449 |
| A | HOH810 |
| A | HOH841 |
| A | HOH953 |
| A | HOH1031 |
| A | HOH1039 |
| A | HOH1053 |
| B | ARG326 |
| A | LEU164 |
| B | GLN328 |
| B | ILE345 |
| B | HIS348 |
| B | GLN420 |
| B | THR421 |
| B | GLY424 |
| B | HOH825 |
| B | HOH846 |
| A | THR165 |
| A | GLY170 |
| A | SER171 |
| A | PHE196 |
| A | ILE197 |
| A | THR198 |
| A | ILE442 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 702 |
| Chain | Residue |
| A | LYS527 |
| A | ASP600 |
| A | ASN601 |
| A | HOH982 |
| A | HOH1078 |
| site_id | AC3 |
| Number of Residues | 29 |
| 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 | HOH833 |
| A | HOH840 |
| A | HOH892 |
| 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 | HOH874 |
| B | HOH905 |
| B | HOH974 |
| B | HOH991 |
| B | HOH1062 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 702 |
| Chain | Residue |
| A | LYS82 |
| A | ARG85 |
| A | HOH848 |
| B | THR564 |
| B | HOH824 |
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 |
