NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B. Determined by solution NMR. Released 20 May 2008.
Explore 2JSS in 3D Show helices and sheets RCSB PDB PDBe
2JSS contains 14 α-helices and 0 β-strands across 2 chains. 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 | 6-16 | 11 | |
| α-helix | 24-50 | 27 | |
| α-helix | 59-69 | 11 | |
| α-helix | 73-92 | 20 | |
| α-helix | 98-101 | 4 | |
| α-helix | 108-117 | 10 | |
| α-helix | 130-155 | 26 | |
| α-helix | 162-170 | 9 | |
| α-helix | 173-179 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-16 | 5 | |
| α-helix | 23-26 | 4 | |
| α-helix | 34-36 | 3 | |
| α-helix | 53-56 | 4 | |
| α-helix | 57-61 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chimera of Histone H2B.1 and Histone H2A.Z | A | protein | 192 | Saccharomyces cerevisiae | P02293 (AlphaFold model), Q12692 (AlphaFold model) |
| Uncharacterized protein YER030W | B | protein | 62 | Saccharomyces cerevisiae | P40019 (AlphaFold model) |
>2JSS_1 Chimera of Histone H2B.1 and Histone H2A.Z (chains A) RKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAR EIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQAQSSSARAGLQFPVGRIKRYLKRHAT GRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIR ATIASGGVLPHI
>2JSS_2 Uncharacterized protein YER030W (chains B) TVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEELDK KE
NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. Zhou, Z., Feng, H., Hansen, D.F. et al. Nat Struct Mol Biol (2008) 15:868-869. DOI 10.1038/nsmb.1465 · PubMed
Other PDB entries of the same protein (UniProt P02293 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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