The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded. Determined by solution NMR. Released 28 Mar 2006.
Explore 1YZC in 3D Show helices and sheets RCSB PDB PDBe
1YZC contains 3 α-helices and 0 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 | 24-40 | 17 | |
| α-helix | 57-81 | 25 | |
| α-helix | 84-97 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| edesigned apo-cytochrome b562 | A | protein | 106 | Homo sapiens | Q0SXH8 (AlphaFold model) |
>1YZC_1 edesigned apo-cytochrome b562 (chains A) ADLEDNDETGNDNGKGGEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTGRAGNQKGG
A protein folding pathway with multiple folding intermediates at atomic resolution. Feng, H., Zhou, Z., Bai, Y. Proc Natl Acad Sci U S A (2005) 102:5026-5031. DOI 10.1073/pnas.0501372102 · PubMed
Other PDB entries of the same protein (UniProt Q0SXH8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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