Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K). Determined by solution NMR. Released 20 May 2015.
Explore 2RUF in 3D Show helices and sheets RCSB PDB PDBe
2RUF contains 3 α-helices and 5 β-strands across 1 chain. 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 | 10-11 | 2 | 1 |
| α-helix | 17-22 | 6 | |
| β-strand | 27-33 | 7 | 1 |
| α-helix | 38-56 | 19 | |
| β-strand | 63-69 | 7 | 1 |
| β-strand | 84-88 | 5 | 1 |
| β-strand | 97-98 | 2 | 1 |
| α-helix | 105-115 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein disulfide-isomerase | A | protein | 121 | Humicola insolens | P55059 (AlphaFold model) |
>2RUF_1 Protein disulfide-isomerase (chains A) GPLGSEGPVTVVVAKNYNEIVLDDTKDVLIEFYAPWCGHCKALAPKYEELGALYAKSEFK DRVVIAKVDATANDVPDEIQGFPTIKLYPAGAKGQPVTYSGSRTVEDLIKFIAENGKYKA A
Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase. Inagaki, K., Satoh, T., Yagi-Utsumi, M. et al. FEBS Lett (2015) 589:2690-2694. DOI 10.1016/j.febslet.2015.07.041 · PubMed
Other PDB entries of the same protein (UniProt P55059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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