2OUG: RfaH transcription factor

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.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Escherichia coli
Chains
4
Atoms
4,981
Mol. weight
73.46 kDa
Released
1 May 2007

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

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix14-2310
β-strand27-2931
β-strand32-3872
β-strand43-4972
β-strand54-5961
α-helix66-716
β-strand75-7841
α-helix86-872
α-helix91-988
α-helix118-12912
α-helix135-15521
Chain B: 6 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand3-973
α-helix14-2310
β-strand27-2933
β-strand32-3874
β-strand43-4974
β-strand54-5963
α-helix66-716
β-strand75-7843
β-strand8015
β-strand8615
α-helix871
α-helix91-988
α-helix119-12911
α-helix135-15521
Chain C: 6 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand3-976
α-helix14-2310
β-strand27-2936
β-strand32-3877
β-strand43-4977
β-strand54-5966
α-helix66-716
β-strand75-7846
α-helix86-872
α-helix91-988
α-helix119-12911
α-helix135-15521
Chain D: 6 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand3-978
α-helix14-2310
β-strand27-2938
β-strand32-3659
β-strand45-4959
β-strand54-5968
α-helix66-716
β-strand75-7848
α-helix86-872
α-helix91-988
α-helix119-12911
α-helix135-15521

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcriptional activator rfaHA, B, C, Dprotein162Escherichia coliP0AFW0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2OUG_1 Transcriptional activator rfaH (chains A, B, C, D)
MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFD
PEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITE
GAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL

Primary citation

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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