The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N-terminal helix unfolded. Determined by solution NMR. Released 28 Aug 2005.
Explore 1YZA in 3D Show helices and sheets RCSB PDB PDBe
1YZA contains 4 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 | 23-42 | 20 | |
| α-helix | 47-50 | 4 | |
| α-helix | 57-80 | 24 | |
| α-helix | 84-105 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Redesigned apo-cytochrome b562 | A | protein | 106 | Homo sapiens | Q0SXH8 (AlphaFold model) |
>1YZA_1 Redesigned apo-cytochrome b562 (chains A) ADLEDNDETGNDNGKGGEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTIRAYNQKYG
Specific non-native hydrophobic interactions in a hidden folding intermediate: implication for protein folding. Feng, H., Takei, T., Lipsitz, R. et al. Biochemistry (2003) 42:12461-12465. DOI 10.1021/bi035561s · 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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