2JSS: Chaperone Chz1

NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B. Determined by solution NMR. Released 20 May 2008.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
1,965
Mol. weight
28.03 kDa
Released
20 May 2008

Explore 2JSS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix6-1611
α-helix24-5027
α-helix59-6911
α-helix73-9220
α-helix98-1014
α-helix108-11710
α-helix130-15526
α-helix162-1709
α-helix173-1797
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix12-165
α-helix23-264
α-helix34-363
α-helix53-564
α-helix57-615

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chimera of Histone H2B.1 and Histone H2A.ZAprotein192Saccharomyces cerevisiaeP02293 (AlphaFold model), Q12692 (AlphaFold model)
Uncharacterized protein YER030WBprotein62Saccharomyces cerevisiaeP40019 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JSS_1 Chimera of Histone H2B.1 and Histone H2A.Z (chains A)
RKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAR
EIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQAQSSSARAGLQFPVGRIKRYLKRHAT
GRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIR
ATIASGGVLPHI
Sequence of entity 2 (B), FASTA
>2JSS_2 Uncharacterized protein YER030W (chains B)
TVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEELDK
KE

Primary citation

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:

Browse structure collections

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