Dimeric horse cytochrome c formed by refolding from molten globule state. Determined by X-ray diffraction at 1.8 Å resolution. Released 16 Jul 2014.
Explore 3WUI in 3D Show helices and sheets RCSB PDB PDBe
3WUI contains 9 α-helices and 2 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 |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 24-26 | 3 | |
| α-helix | 38 | 1 | |
| β-strand | 39 | 1 | 1 |
| α-helix | 50-54 | 5 | |
| α-helix | 57 | 1 | |
| β-strand | 58 | 1 | 1 |
| α-helix | 59 | 1 | |
| α-helix | 61-69 | 9 | |
| α-helix | 71-74 | 4 | |
| α-helix | 88-101 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytochrome c | A | protein | 104 | Equus caballus | P00004 (AlphaFold model) |
>3WUI_1 Cytochrome c (chains A) GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
Water and common crystallization additives (PG4, PEG) are not listed.
Formation of domain-swapped oligomer of cytochrome C from its molten globule state oligomer. Deshpande, M.S., Parui, P.P., Kamikubo, H. et al. Biochemistry (2014) 53:4696-4703. DOI 10.1021/bi500497s · PubMed
Other PDB entries of the same protein (UniProt P00004 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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