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.
Explore 2FHS in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 1 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 42-44 | 3 | |
| α-helix | 45-54 | 10 | |
| β-strand | 60-62 | 3 | 1 |
| α-helix | 68-81 | 14 | |
| 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 | 135-136 | 2 | |
| β-strand | 139-145 | 7 | 1 |
| α-helix | 147-149 | 3 | |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 182-189 | 8 | 1 |
| α-helix | 190-191 | 2 | |
| α-helix | 201-213 | 13 | |
| α-helix | 222-233 | 12 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 1 |
| α-helix | 251-253 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 2 |
| α-helix | 20-30 | 11 | |
| β-strand | 34-39 | 6 | 2 |
| α-helix | 42-54 | 13 | |
| β-strand | 60-62 | 3 | 2 |
| α-helix | 68-81 | 14 | |
| β-strand | 85-90 | 6 | 2 |
| α-helix | 104-107 | 4 | |
| α-helix | 110-116 | 7 | |
| α-helix | 117-122 | 6 | |
| α-helix | 123-131 | 9 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-145 | 11 | 2 |
| α-helix | 147-149 | 3 | |
| α-helix | 158-177 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 183-189 | 7 | 2 |
| α-helix | 190-191 | 2 | |
| α-helix | 204-213 | 10 | |
| α-helix | 222-232 | 11 | |
| α-helix | 235-237 | 3 | |
| β-strand | 244-247 | 4 | 2 |
| α-helix | 251-253 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| α-helix | 38-40 | 3 | |
| α-helix | 41-50 | 10 | |
| α-helix | 67-69 | 3 | |
| α-helix | 72-75 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| enoyl-[acyl-carrier-protein] reductase, NADH-dependent | A, B | protein | 262 | Escherichia coli | P0AEK4 (AlphaFold model) |
| Acyl carrier protein | C | protein | 78 | Escherichia coli | P0A6A8 (AlphaFold model) |
>2FHS_1 enoyl-[acyl-carrier-protein] reductase, NADH-dependent (chains A, B) MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIV LQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDIS SYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPE GVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGI SGEVVHVDGGFSIAAMNELELK
>2FHS_2 Acyl carrier protein (chains C) MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA EKITTVQAAIDYINGHQA
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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