1QSG: Enoyl reductase inhibition by triclosan
Crystal structure of enoyl reductase inhibition by triclosan. Determined by X-ray diffraction at 1.75 Å resolution. Released 21 Jul 1999.
- Method
- X-ray diffraction
- Resolution
- 1.75 Å
- Organism
- Escherichia coli
- Chains
- 8
- Atoms
- 17,287
- Mol. weight
- 234.47 kDa
- Ligands
- TCL, NAD, GLC
- Released
- 21 Jul 1999
Explore 1QSG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1QSG contains 145 α-helices and 72 β-strands across 8 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.
Chain A: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 1 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 45-54 | 10 | |
| β-strand | 60-62 | 3 | 1 |
| α-helix | 68-79 | 12 | |
| β-strand | 85-90 | 6 | 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 | 135-145 | 11 | 1 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 2 |
| α-helix | 158-177 | 20 | |
| β-strand | 182-189 | 8 | 1 |
| α-helix | 190-191 | 2 | |
| α-helix | 197-199 | 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 | |
| β-strand | 254 | 1 | 3 |
Chain B: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 4 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 4 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 4 |
| α-helix | 68-78 | 11 | |
| β-strand | 85-90 | 6 | 4 |
| 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 | 135-145 | 11 | 4 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 5 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 4 |
| α-helix | 190-191 | 2 | |
| α-helix | 196-199 | 4 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 4 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 6 |
Chain C: 19 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 7 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 7 |
| α-helix | 42-44 | 3 | |
| α-helix | 45-54 | 10 | |
| β-strand | 60-62 | 3 | 7 |
| α-helix | 68-79 | 12 | |
| β-strand | 85-90 | 6 | 7 |
| 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 | 135-145 | 11 | 7 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 6 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 183-189 | 7 | 7 |
| α-helix | 190-191 | 2 | |
| α-helix | 196-199 | 4 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 7 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 5 |
Chain D: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 8 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 8 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 8 |
| α-helix | 68-81 | 14 | |
| β-strand | 85-90 | 6 | 8 |
| 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 | 135-145 | 11 | 8 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 3 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 8 |
| α-helix | 190-191 | 2 | |
| α-helix | 196-199 | 4 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 8 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 2 |
Chain E: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 9 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 9 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 9 |
| α-helix | 68-79 | 12 | |
| β-strand | 85-90 | 6 | 9 |
| α-helix | 97-99 | 3 | |
| 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 | 135-145 | 11 | 9 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 10 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 9 |
| α-helix | 190-191 | 2 | |
| α-helix | 197-199 | 3 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 9 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 11 |
Chain F: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 12 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 12 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 12 |
| α-helix | 68-81 | 14 | |
| β-strand | 85-90 | 6 | 12 |
| 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 | 135-145 | 11 | 12 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 13 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 12 |
| α-helix | 190-191 | 2 | |
| α-helix | 196-199 | 4 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-233 | 12 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 12 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 14 |
Chain G: 19 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 15 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 15 |
| α-helix | 45-54 | 10 | |
| β-strand | 60-62 | 3 | 15 |
| α-helix | 68-79 | 12 | |
| β-strand | 85-90 | 6 | 15 |
| 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 | 135-145 | 11 | 15 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 14 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 15 |
| α-helix | 190-191 | 2 | |
| α-helix | 197-199 | 3 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 15 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 13 |
| α-helix | 257-259 | 3 | |
Chain H: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 16 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 16 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 16 |
| α-helix | 68-78 | 11 | |
| β-strand | 85-90 | 6 | 16 |
| 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 | 135-145 | 11 | 16 |
| α-helix | 147-149 | 3 | |
| β-strand | 152 | 1 | 11 |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 16 |
| α-helix | 190-191 | 2 | |
| α-helix | 197-199 | 3 | |
| α-helix | 203-213 | 11 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 16 |
| α-helix | 251-253 | 3 | |
| β-strand | 254 | 1 | 10 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Enoyl-[acyl-carrier-protein] reductase | A, B, C, D, E, F, G, H | protein | 265 | Escherichia coli | P0AEK4 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>1QSG_1 ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE (chains A, B, C, D, E, F, G, H)
GSHMGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGS
DIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAH
DISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAM
GPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLS
AGISGEVVHVDGGFSIAAMNELELK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| TCL | Triclosan | C12 H7 Cl3 O2 | 8 |
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 8 |
| GLC | alpha-D-glucopyranose | C6 H12 O6 | 8 |
Primary citation
Structural basis and mechanism of enoyl reductase inhibition by triclosan. Stewart, M.J., Parikh, S., Xiao, G. et al. J Mol Biol (1999) 290:859-865. DOI 10.1006/jmbi.1999.2907 · PubMed
Other PDB entries of the same protein (UniProt P0AEK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7UMW 1.54 Å, Crystal structure of E. Coli FabI in complex with NAD and Fabimycin…
- 7UM8 1.7 Å, Crystal structure of E. Coli FabI in complex with NAD and…
- 4CV2 1.8 Å, Crystal structure of E. coli FabI in complex with NADH and CG400549
- 1QG6 1.9 Å, Crystal structure of E. Coli enoyl acyl carrier protein reductase in complex with NAD…
- 3PJF 1.9 Å, Structure of ENR G93V mutant-NAD+-triclosan complex
- 4CV3 1.95 Å, Crystal structure of E. coli FabI in complex with NADH and PT166
- 5CFZ 1.97 Å, Crystal structure of E. coli FabI in apo form
- 1C14 2.0 Å, Crystal structure of E coli enoyl reductase-NAD+-triclosan complex
- 4D46 2.0 Å, Crystal structure of E. coli FabI in complex with NAD and…
- 5CG1 2.07 Å, Crystal structure of E. coli FabI bound to the carbamoylated benzodiazaborine inhibitor…
- 1DFI 2.09 Å, X-ray structure of escherichia coli enoyl reductase with bound NAD
- 5CG2 2.11 Å, Crystal structure of E. coli FabI bound to the thiocarbamoylated benzodiazaborine…
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