2LY8: Budding yeast chaperone Scm3

The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant. Determined by solution NMR. Released 12 Dec 2012.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
966
Mol. weight
13.72 kDa
Released
12 Dec 2012

Explore 2LY8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LY8 contains 5 α-helices and 2 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.

Chain A: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix6-1813
β-strand2711
α-helix29-5325
α-helix69-9426
β-strand10011
α-helix102-11110
α-helix115-1184

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Budding yeast chaperone Scm3Aprotein121Saccharomyces cerevisiaeP36012 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LY8_1 Budding yeast chaperone Scm3 (chains A)
LISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHTNLLALHLVPR
GSKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFG
G

Primary citation

Identification of Functionally Conserved Regions in the Structure of the Chaperone/CenH3/H4 Complex. Hong, J., Feng, H., Zhou, Z. et al. J Mol Biol (2013) 425:536-545. DOI 10.1016/j.jmb.2012.11.021 · PubMed

Other PDB entries of the same protein (UniProt P36012 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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