2L5A: PDB entry 2L5A

Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3. Determined by solution NMR. Released 16 Mar 2011.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
1,803
Mol. weight
27.03 kDa
Released
16 Mar 2011

Explore 2L5A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2L5A contains 12 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.

Chain A: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix6-1611
α-helix20-223
α-helix29-5527
α-helix61-633
α-helix66-716
α-helix85-10521
α-helix137-1393
α-helix145-15511
α-helix172-19120
α-helix192-1965
α-helix197-1982
α-helix206-22015

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3-like centromeric protein CSE4, Protein SCM3, Histone H4Aprotein235Saccharomyces cerevisiaeP02309 (AlphaFold model), P36012 (AlphaFold model), Q12334 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2L5A_1 Histone H3-like centromeric protein CSE4, Protein SCM3, Histone H4 (chains A)
MHHHHHHKKLLISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHT
NLLALHAKRITIMKKDMQLARRIRGQFLVPRGSMERHKLADENMRKVWSNIISKYESIEE
QGDLVDLKTGEIVEDNGHIKTLTANNSTKDKRTKYTSVLRDIIDISDEEDGDKGGVKRIS
GLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG

Primary citation

Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. Zhou, Z., Feng, H., Zhou, B.R. et al. Nature (2011) 472:234-237. DOI 10.1038/nature09854 · PubMed

Other PDB entries of the same protein (UniProt P02309 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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