Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences. Determined by solution NMR. Released 16 May 2006.
Explore 1ZW7 in 3D Show helices and sheets RCSB PDB PDBe
1ZW7 contains 5 α-helices and 9 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 | 3-6 | 4 | 1 |
| β-strand | 13-15 | 3 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-28 | 6 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-43 | 2 | 3 |
| β-strand | 44 | 1 | 4 |
| β-strand | 49 | 1 | 4 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 2 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-68 | 3 | 1 |
| β-strand | 69-70 | 2 | 3 |
| α-helix | 77-79 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin | A | protein | 82 | Saccharomyces cerevisiae | P0CG63 (AlphaFold model) |
>1ZW7_1 Ubiquitin (chains A) MQIFVKTLTGATITLEVESSDTIDNVKSKIQAAPGIPPDQQELIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGGHHHHHH
Elimination of the C-cap in ubiquitin-structure, dynamics and thermodynamic consequences. Ermolenko, D.N., Dangi, B., Gvritishvili, A. et al. Biophys Chem (2007) 126:25-35. DOI 10.1016/j.bpc.2006.03.017 · PubMed
Other PDB entries of the same protein (UniProt P0CG63 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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