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

ElementResiduesLengthSheet
β-strand8-1141
α-helix20-3011
β-strand34-3961
α-helix45-5410
β-strand60-6231
α-helix68-7912
β-strand85-9061
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145111
α-helix147-1493
β-strand15212
α-helix158-17720
β-strand182-18981
α-helix190-1912
α-helix197-1993
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-24741
α-helix251-2533
β-strand25413
Chain B: 18 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-1144
α-helix20-3011
β-strand34-3964
α-helix42-5413
β-strand60-6234
α-helix68-7811
β-strand85-9064
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145114
α-helix147-1493
β-strand15215
α-helix158-17720
α-helix178-1803
β-strand182-18984
α-helix190-1912
α-helix196-1994
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-24744
α-helix251-2533
β-strand25416
Chain C: 19 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-1147
α-helix20-3011
β-strand34-3967
α-helix42-443
α-helix45-5410
β-strand60-6237
α-helix68-7912
β-strand85-9067
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145117
α-helix147-1493
β-strand15216
α-helix158-17720
α-helix178-1803
β-strand183-18977
α-helix190-1912
α-helix196-1994
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-24747
α-helix251-2533
β-strand25415
Chain D: 18 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-1148
α-helix20-3011
β-strand34-3968
α-helix42-5413
β-strand60-6238
α-helix68-8114
β-strand85-9068
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145118
α-helix147-1493
β-strand15213
α-helix158-17720
α-helix178-1803
β-strand182-18988
α-helix190-1912
α-helix196-1994
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-24748
α-helix251-2533
β-strand25412
Chain E: 18 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-1149
α-helix20-3011
β-strand34-3969
α-helix42-5413
β-strand60-6239
α-helix68-7912
β-strand85-9069
α-helix97-993
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145119
α-helix147-1493
β-strand152110
α-helix158-17720
α-helix178-1803
β-strand182-18989
α-helix190-1912
α-helix197-1993
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-24749
α-helix251-2533
β-strand254111
Chain F: 18 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-11412
α-helix20-3011
β-strand34-39612
α-helix42-5413
β-strand60-62312
α-helix68-8114
β-strand85-90612
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-1451112
α-helix147-1493
β-strand152113
α-helix158-17720
α-helix178-1803
β-strand182-189812
α-helix190-1912
α-helix196-1994
α-helix203-21311
α-helix222-23312
α-helix235-2373
β-strand244-247412
α-helix251-2533
β-strand254114
Chain G: 19 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-11415
α-helix20-3011
β-strand34-39615
α-helix45-5410
β-strand60-62315
α-helix68-7912
β-strand85-90615
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-1451115
α-helix147-1493
β-strand152114
α-helix158-17720
α-helix178-1803
β-strand182-189815
α-helix190-1912
α-helix197-1993
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-247415
α-helix251-2533
β-strand254113
α-helix257-2593
Chain H: 18 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-11416
α-helix20-3011
β-strand34-39616
α-helix42-5413
β-strand60-62316
α-helix68-7811
β-strand85-90616
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-1451116
α-helix147-1493
β-strand152111
α-helix158-17720
α-helix178-1803
β-strand182-189816
α-helix190-1912
α-helix197-1993
α-helix203-21311
α-helix222-23211
α-helix235-2373
β-strand244-247416
α-helix251-2533
β-strand254110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Enoyl-[acyl-carrier-protein] reductaseA, B, C, D, E, F, G, Hprotein265Escherichia coliP0AEK4 (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

IDNameFormulaCopies
TCLTriclosanC12 H7 Cl3 O28
NADNicotinamide-adenine-dinucleotideC21 H27 N7 O14 P28
GLCalpha-D-glucopyranoseC6 H12 O68

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:

Browse structure collections

About this viewer

MolViewer shows 1QSG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.