E. coli Enoyl Reductase in complex with NAD and SB611113. Determined by X-ray diffraction at 2.33 Å resolution. Released 6 May 2003.
Explore 1MFP in 3D Show helices and sheets RCSB PDB PDBe
1MFP contains 41 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 1 |
| α-helix | 20-30 | 11 | |
| α-helix | 33 | 1 | |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 42-44 | 3 | |
| α-helix | 45-53 | 9 | |
| β-strand | 60-62 | 3 | 1 |
| α-helix | 68-81 | 14 | |
| β-strand | 85 | 1 | 2 |
| β-strand | 88-90 | 3 | 1 |
| α-helix | 97-100 | 4 | |
| α-helix | 104-107 | 4 | |
| α-helix | 110-117 | 8 | |
| α-helix | 118-122 | 5 | |
| α-helix | 123-131 | 9 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135 | 1 | 2 |
| α-helix | 136 | 1 | |
| β-strand | 140-145 | 6 | 1 |
| α-helix | 147-149 | 3 | |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 183-189 | 7 | 1 |
| α-helix | 190-191 | 2 | |
| α-helix | 195-197 | 3 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 1 |
| α-helix | 251-253 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1008-1011 | 4 | 3 |
| α-helix | 1020-1030 | 11 | |
| α-helix | 1033 | 1 | |
| β-strand | 1034-1039 | 6 | 3 |
| α-helix | 1042-1054 | 13 | |
| β-strand | 1060-1062 | 3 | 3 |
| α-helix | 1068-1081 | 14 | |
| β-strand | 1085 | 1 | 4 |
| β-strand | 1088-1090 | 3 | 3 |
| α-helix | 1097-1100 | 4 | |
| α-helix | 1104-1107 | 4 | |
| α-helix | 1110-1117 | 8 | |
| α-helix | 1118-1122 | 5 | |
| α-helix | 1123-1131 | 9 | |
| α-helix | 1132-1134 | 3 | |
| β-strand | 1135 | 1 | 4 |
| α-helix | 1136 | 1 | |
| β-strand | 1139-1145 | 7 | 3 |
| α-helix | 1147-1149 | 3 | |
| α-helix | 1157-1177 | 21 | |
| α-helix | 1178-1180 | 3 | |
| β-strand | 1182-1189 | 8 | 3 |
| α-helix | 1190-1191 | 2 | |
| α-helix | 1195-1198 | 4 | |
| α-helix | 1203-1213 | 11 | |
| α-helix | 1222-1232 | 11 | |
| α-helix | 1235-1237 | 3 | |
| β-strand | 1244-1247 | 4 | 3 |
| α-helix | 1251-1253 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| enoyl-[acyl-carrier-protein] reductase [Nadh] | A, B | protein | 262 | Escherichia coli | P0AEK4 (AlphaFold model) |
>1MFP_1 enoyl-[acyl-carrier-protein] reductase [Nadh] (chains A, B) MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIV LQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDIS SYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPE GVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGI SGEVVHVDGGFSIAAMNELELK
| ID | Name | Formula | Copies |
|---|---|---|---|
| IDN | (e)-N-methyl-N-(1-methyl-1H-indol-3-ylmethyl)-3-(7-oxo-5,6,7,8-tetrahydro-[1,8]… | C22 H22 N4 O2 | 2 |
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 2 |
Water and common crystallization additives (SO4) are not listed.
Indole Naphthyridinones as Inhibitors of Bacterial Enoyl-ACP Reductases FabI and FabK. Seefeld, M.A., Miller, W.H., Newlander, K.A. et al. J Med Chem (2003) 46:1627-1635. DOI 10.1021/jm0204035 · PubMed
Other PDB entries of the same protein (UniProt P0AEK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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