2FHS: Acyl Carrier Protein

Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Oct 2006.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Escherichia coli
Chains
3
Atoms
4,020
Mol. weight
64.43 kDa
Released
17 Oct 2006

Explore 2FHS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FHS contains 39 α-helices and 14 β-strands across 3 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: 18 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand8-1141
α-helix20-3011
β-strand34-3961
α-helix42-443
α-helix45-5410
β-strand60-6231
α-helix68-8114
β-strand88-9031
α-helix97-1004
α-helix104-1074
α-helix110-1178
α-helix118-1225
α-helix123-1319
α-helix135-1362
β-strand139-14571
α-helix147-1493
α-helix158-17720
α-helix178-1803
β-strand182-18981
α-helix190-1912
α-helix201-21313
α-helix222-23312
α-helix235-2373
β-strand244-24741
α-helix251-2533
Chain B: 16 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand8-1142
α-helix20-3011
β-strand34-3962
α-helix42-5413
β-strand60-6232
α-helix68-8114
β-strand85-9062
α-helix104-1074
α-helix110-1167
α-helix117-1226
α-helix123-1319
α-helix132-1343
β-strand135-145112
α-helix147-1493
α-helix158-17720
α-helix178-1803
β-strand183-18972
α-helix190-1912
α-helix204-21310
α-helix222-23211
α-helix235-2373
β-strand244-24742
α-helix251-2533
Chain C: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74
α-helix38-403
α-helix41-5010
α-helix67-693
α-helix72-754

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
enoyl-[acyl-carrier-protein] reductase, NADH-dependentA, Bprotein262Escherichia coliP0AEK4 (AlphaFold model)
Acyl carrier proteinCprotein78Escherichia coliP0A6A8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2FHS_1 enoyl-[acyl-carrier-protein] reductase, NADH-dependent (chains A, B)
MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIV
LQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDIS
SYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPE
GVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGI
SGEVVHVDGGFSIAAMNELELK
Sequence of entity 2 (C), FASTA
>2FHS_2 Acyl carrier protein (chains C)
MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA
EKITTVQAAIDYINGHQA

Primary citation

Structure of Acyl Carrier Protein Bound to FabI, the FASII Enoyl Reductase from Escherichia coli. Rafi, S., Novichenok, P., Kolappan, S. et al. J Biol Chem (2006) 281:39285-39293. DOI 10.1074/jbc.M608758200 · 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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