6AHE
Crystal structure of enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD and AFN-1252
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue NAD A 300 |
| Chain | Residue |
| A | GLY15 |
| A | ILE94 |
| A | GLY95 |
| A | ILE121 |
| A | LEU147 |
| A | THR148 |
| A | LYS166 |
| A | ALA192 |
| A | GLY193 |
| A | PRO194 |
| A | ILE195 |
| A | ALA17 |
| A | THR197 |
| A | ALA199 |
| A | 0WE301 |
| A | HOH407 |
| A | SER21 |
| A | ILE22 |
| A | PRO42 |
| A | CYS65 |
| A | ASP66 |
| A | VAL67 |
| A | SER93 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue NAD D 300 |
| Chain | Residue |
| D | GLY15 |
| D | VAL16 |
| D | ALA17 |
| D | SER21 |
| D | ILE22 |
| D | PRO42 |
| D | CYS65 |
| D | ASP66 |
| D | VAL67 |
| D | SER93 |
| D | ILE94 |
| D | GLY95 |
| D | LEU147 |
| D | THR148 |
| D | LYS166 |
| D | ALA192 |
| D | GLY193 |
| D | PRO194 |
| D | ILE195 |
| D | THR197 |
| D | LEU198 |
| D | ALA199 |
| D | 0WE301 |
| D | HOH406 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue NAD C 300 |
| Chain | Residue |
| C | GLY15 |
| C | ALA17 |
| C | SER21 |
| C | ILE22 |
| C | PRO42 |
| C | CYS65 |
| C | ASP66 |
| C | VAL67 |
| C | SER93 |
| C | ILE94 |
| C | GLY95 |
| C | ILE121 |
| C | LEU147 |
| C | THR148 |
| C | LYS166 |
| C | ALA192 |
| C | GLY193 |
| C | PRO194 |
| C | ILE195 |
| C | THR197 |
| C | LEU198 |
| C | ALA199 |
| C | 0WE301 |
| C | HOH402 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 300 |
| Chain | Residue |
| B | GLY15 |
| B | VAL16 |
| B | ALA17 |
| B | SER21 |
| B | ILE22 |
| B | PRO42 |
| B | CYS65 |
| B | ASP66 |
| B | VAL67 |
| B | SER93 |
| B | ILE94 |
| B | GLY95 |
| B | ILE121 |
| B | LEU147 |
| B | THR148 |
| B | LYS166 |
| B | ALA192 |
| B | GLY193 |
| B | PRO194 |
| B | ILE195 |
| B | THR197 |
| B | ALA199 |
| B | 0WE301 |
