Crystal structure of the conserved central domain of yeast Spn1/Iws1. Determined by X-ray diffraction at 1.85 Å resolution. Released 13 Oct 2010.
Explore 3NFQ in 3D Show helices and sheets RCSB PDB PDBe
3NFQ contains 21 α-helices and 0 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 10-42 | 33 | |
| α-helix | 51-63 | 13 | |
| α-helix | 66-68 | 3 | |
| α-helix | 69-74 | 6 | |
| α-helix | 77-85 | 9 | |
| α-helix | 87-88 | 2 | |
| α-helix | 96-107 | 12 | |
| α-helix | 113-119 | 7 | |
| α-helix | 121-130 | 10 | |
| α-helix | 136-149 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-42 | 34 | |
| α-helix | 51-63 | 13 | |
| α-helix | 66-68 | 3 | |
| α-helix | 69-74 | 6 | |
| α-helix | 77-85 | 9 | |
| α-helix | 87-88 | 2 | |
| α-helix | 92-95 | 4 | |
| α-helix | 96-108 | 13 | |
| α-helix | 113-119 | 7 | |
| α-helix | 121-130 | 10 | |
| α-helix | 136-149 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor IWS1 | A, B | protein | 170 | Saccharomyces cerevisiae | Q06505 (AlphaFold model) |
>3NFQ_1 Transcription factor IWS1 (chains A, B) RRTRRDEDDLEQYLDEKILRLKDEMNIAAQLDIDTLNKRIETGDTSLIAMQKVKLLPKVV SVLSKANLADTILDNNLLQSVRIWLEPLPDGSLPSFEIQKSLFAALNDLPVKTEHLKESG LGRVVIFYTKSKRVEAQLARLAEKLIAEWTRPIIGASDNYRDKRIMQLEF
The Transcription Factor Spn1 Regulates Gene Expression via a Highly Conserved Novel Structural Motif. Pujari, V., Radebaugh, C.A., Chodaparambil, J.V. et al. J Mol Biol (2010) 404:1-15. DOI 10.1016/j.jmb.2010.09.040 · PubMed
Other PDB entries of the same protein (UniProt Q06505 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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