Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0071768 | biological_process | mycolic acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue 9VZ A 301 |
| Chain | Residue |
| A | GLY96 |
| A | PHE97 |
| A | MET98 |
| A | MET103 |
| A | PHE149 |
| A | MET161 |
| A | MET199 |
| A | LEU207 |
| A | NAD302 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | binding site for residue NAD A 302 |
| Chain | Residue |
| A | GLY14 |
| A | ILE15 |
| A | ILE16 |
| A | SER20 |
| A | ILE21 |
| A | PHE41 |
| A | LEU63 |
| A | ASP64 |
| A | VAL65 |
| A | SER94 |
| A | ILE95 |
| A | GLY96 |
| A | ILE122 |
| A | MET147 |
| A | ASP148 |
| A | PHE149 |
| A | LYS165 |
| A | ALA191 |
| A | GLY192 |
| A | PRO193 |
| A | ILE194 |
| A | THR196 |
| A | 9VZ301 |
| A | HOH402 |
| A | HOH406 |
| A | HOH416 |
| A | HOH432 |
| A | HOH469 |
| A | HOH483 |
| A | HOH497 |
| A | HOH509 |
| A | HOH531 |
| A | HOH536 |
| A | HOH593 |
| A | HOH601 |
| A | HOH603 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue ETX A 303 |
| Chain | Residue |
| A | SER19 |
| A | HIS24 |
| A | ILE194 |
| A | LYS233 |
| A | ASP234 |
| A | ALA235 |
| A | THR236 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ETX A 304 |
| Chain | Residue |
| A | ASP150 |
| A | SER152 |
| A | SER152 |
| A | ARG153 |
| A | TYR259 |
| A | HIS265 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ETX A 305 |
| Chain | Residue |
| A | SER19 |
| A | SER19 |
| A | ARG195 |
| A | ARG195 |
| A | THR196 |
| A | SER200 |
| A | SER200 |
| A | HOH577 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | SER20 | |
| A | ASP64 | |
| A | ILE95 | |
| A | LYS165 | |
| A | ILE194 | |
| Chain | Residue | Details |
| A | TYR158 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 |
| Chain | Residue | Details |
| A | PHE149 | |
| Chain | Residue | Details |
| A | TYR158 | |
| Chain | Residue | Details |
| A | THR266 | |
