5TRT
Crystal Structure of enoyl-(acyl carrier protein) reductase from Burkholderia pseudomallei 1710b bound to NAD
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 | 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 | 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 | 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 | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | GLU223 |
| A | HOH491 |
| D | HOH538 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLU58 |
| A | VAL60 |
| A | HIS81 |
| A | HOH556 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 303 |
| Chain | Residue |
| A | ILE20 |
| A | VAL40 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
| A | SER91 |
| A | ILE92 |
| A | GLY93 |
| A | LEU144 |
| A | SER145 |
| A | LYS163 |
| A | ALA189 |
| A | GLY190 |
| A | PRO191 |
| A | ILE192 |
| A | HOH414 |
| A | HOH426 |
| A | HOH433 |
| A | HOH437 |
| A | HOH480 |
| A | HOH511 |
| A | HOH552 |
| A | HOH558 |
| A | GLY13 |
| A | LEU15 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ALA76 |
| A | GLU98 |
| A | PRO133 |
| A | HOH404 |
| A | HOH584 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| A | ARG110 |
| B | ALA66 |
| B | ASP67 |
| B | ASP68 |
| B | HOH411 |
| B | HOH494 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | binding site for residue NAD B 302 |
| Chain | Residue |
| B | GLY13 |
| B | LEU15 |
| B | SER19 |
| B | ILE20 |
| B | VAL40 |
| B | CYS63 |
| B | ASP64 |
| B | VAL65 |
| B | SER91 |
| B | ILE92 |
| B | GLY93 |
| B | LEU144 |
| B | SER145 |
| B | TYR146 |
| B | LYS163 |
| B | ALA189 |
| B | GLY190 |
| B | PRO191 |
| B | ILE192 |
| B | EDO303 |
| B | HOH410 |
| B | HOH413 |
| B | HOH420 |
| B | HOH431 |
| B | HOH460 |
| B | HOH471 |
| B | HOH481 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | TYR156 |
| B | NAD302 |
| B | HOH410 |
| B | HOH423 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | ALA66 |
| C | ASP68 |
| C | HOH425 |
| C | HOH533 |
| D | ARG110 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue NAD C 302 |
| Chain | Residue |
| C | HOH431 |
| C | GLY13 |
| C | LEU15 |
| C | SER19 |
| C | ILE20 |
| C | VAL40 |
| C | ASP64 |
| C | VAL65 |
| C | SER91 |
| C | ILE92 |
| C | GLY93 |
| C | LEU144 |
| C | SER145 |
| C | LYS163 |
| C | ALA189 |
| C | GLY190 |
| C | PRO191 |
| C | ILE192 |
| C | HOH409 |
| C | HOH415 |
| C | HOH418 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| C | ARG110 |
| D | ALA66 |
| D | ASP68 |
| D | HOH422 |
| site_id | AD2 |
| Number of Residues | 22 |
| Details | binding site for residue NAD D 302 |
| Chain | Residue |
| D | GLY13 |
| D | LEU15 |
| D | ILE20 |
| D | VAL40 |
| D | CYS63 |
| D | ASP64 |
| D | VAL65 |
| D | SER91 |
| D | ILE92 |
| D | GLY93 |
| D | ILE119 |
| D | LEU144 |
| D | SER145 |
| D | LYS163 |
| D | ALA189 |
| D | GLY190 |
| D | PRO191 |
| D | ILE192 |
| D | HOH420 |
| D | HOH423 |
| D | HOH456 |
| D | HOH463 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| A | ASN252 |
| A | HOH458 |
| D | GLU150 |
| D | HOH449 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| A | HOH438 |
| D | ASN252 |
| D | HOH416 |
| D | HOH430 |
| D | HOH453 |
