Crystal structure of the RfaH transcription factor at 2.1A resolution. Determined by X-ray diffraction at 2.1 Å resolution. Released 1 May 2007.
Explore 2OUG in 3D Show helices and sheets RCSB PDB PDBe
2OUG contains 24 α-helices and 26 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 1 |
| α-helix | 14-23 | 10 | |
| β-strand | 27-29 | 3 | 1 |
| β-strand | 32-38 | 7 | 2 |
| β-strand | 43-49 | 7 | 2 |
| β-strand | 54-59 | 6 | 1 |
| α-helix | 66-71 | 6 | |
| β-strand | 75-78 | 4 | 1 |
| α-helix | 86-87 | 2 | |
| α-helix | 91-98 | 8 | |
| α-helix | 118-129 | 12 | |
| α-helix | 135-155 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 3 |
| α-helix | 14-23 | 10 | |
| β-strand | 27-29 | 3 | 3 |
| β-strand | 32-38 | 7 | 4 |
| β-strand | 43-49 | 7 | 4 |
| β-strand | 54-59 | 6 | 3 |
| α-helix | 66-71 | 6 | |
| β-strand | 75-78 | 4 | 3 |
| β-strand | 80 | 1 | 5 |
| β-strand | 86 | 1 | 5 |
| α-helix | 87 | 1 | |
| α-helix | 91-98 | 8 | |
| α-helix | 119-129 | 11 | |
| α-helix | 135-155 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 6 |
| α-helix | 14-23 | 10 | |
| β-strand | 27-29 | 3 | 6 |
| β-strand | 32-38 | 7 | 7 |
| β-strand | 43-49 | 7 | 7 |
| β-strand | 54-59 | 6 | 6 |
| α-helix | 66-71 | 6 | |
| β-strand | 75-78 | 4 | 6 |
| α-helix | 86-87 | 2 | |
| α-helix | 91-98 | 8 | |
| α-helix | 119-129 | 11 | |
| α-helix | 135-155 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 8 |
| α-helix | 14-23 | 10 | |
| β-strand | 27-29 | 3 | 8 |
| β-strand | 32-36 | 5 | 9 |
| β-strand | 45-49 | 5 | 9 |
| β-strand | 54-59 | 6 | 8 |
| α-helix | 66-71 | 6 | |
| β-strand | 75-78 | 4 | 8 |
| α-helix | 86-87 | 2 | |
| α-helix | 91-98 | 8 | |
| α-helix | 119-129 | 11 | |
| α-helix | 135-155 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional activator rfaH | A, B, C, D | protein | 162 | Escherichia coli | P0AFW0 (AlphaFold model) |
>2OUG_1 Transcriptional activator rfaH (chains A, B, C, D) MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFD PEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITE GAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL
Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Belogurov, G.A., Vassylyeva, M.N., Svetlov, V. et al. Mol Cell (2007) 26:117-129. DOI 10.1016/j.molcel.2007.02.021 · PubMed
Other PDB entries of the same protein (UniProt P0AFW0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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