1DFI: Escherichia coli enoyl reductase with bound NAD

X-ray structure of escherichia coli enoyl reductase with bound NAD. Determined by X-ray diffraction at 2.09 Å resolution. Released 28 Jan 1998.

Method
X-ray diffraction
Resolution
2.09 Å
Organism
Escherichia coli
Chains
4
Atoms
7,839
Mol. weight
113.7 kDa
Ligands
NAD
Released
28 Jan 1998

Explore 1DFI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DFI contains 67 α-helices and 40 β-strands across 4 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-helix68-8114
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
α-helix178-1803
β-strand183-18971
α-helix190-1912
α-helix207-2137
α-helix222-23312
α-helix235-2373
β-strand244-24741
α-helix251-2533
β-strand25413
Chain B: 16 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand8-1144
α-helix20-3011
β-strand34-3964
α-helix45-5410
β-strand60-6234
α-helix68-8114
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-helix157-17721
α-helix178-1803
β-strand183-18974
α-helix207-2137
α-helix222-23312
α-helix235-2373
β-strand244-24744
α-helix251-2533
β-strand25416
Chain C: 18 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand8-1147
α-helix20-3011
β-strand34-3967
α-helix42-5413
β-strand60-6237
α-helix68-8114
β-strand8518
β-strand88-9037
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand13518
α-helix1361
β-strand140-14567
α-helix147-1493
β-strand15216
α-helix158-17720
α-helix178-1803
β-strand183-18977
α-helix190-1912
α-helix207-2137
α-helix222-23312
α-helix235-2373
β-strand244-24747
α-helix251-2533
β-strand25415
Chain D: 16 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand8-1149
α-helix20-3011
β-strand34-3969
α-helix42-5413
β-strand60-6239
α-helix68-8114
β-strand85-9069
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix132-1343
β-strand135-145119
α-helix147-1493
β-strand15213
α-helix157-17721
α-helix178-1803
β-strand182-18989
β-strand192110
α-helix207-2137
β-strand220110
α-helix222-23211
α-helix235-2373
β-strand244-24749
α-helix251-2533
β-strand25412

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Enoyl acyl carrier protein reductaseA, B, C, Dprotein261Escherichia coliP0AEK4 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1DFI_1 ENOYL ACYL CARRIER PROTEIN REDUCTASE (chains A, B, C, D)
GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVL
QCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS
YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEG
VRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS
GEVVHVDGGFSIAAMNELELK

Ligands and cofactors

IDNameFormulaCopies
NADNicotinamide-adenine-dinucleotideC21 H27 N7 O14 P24

Primary citation

A mechanism of drug action revealed by structural studies of enoyl reductase. Baldock, C., Rafferty, J.B., Sedelnikova, S.E. et al. Science (1996) 274:2107-2110. DOI 10.1126/science.274.5295.2107 · 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 1DFI 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.