Structural basis for recognition of centromere specific histone H3 variant by nonhistone Scm3. Determined by solution NMR. Released 16 Mar 2011.
Explore 2L5A in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-16 | 11 | |
| α-helix | 20-22 | 3 | |
| α-helix | 29-55 | 27 | |
| α-helix | 61-63 | 3 | |
| α-helix | 66-71 | 6 | |
| α-helix | 85-105 | 21 | |
| α-helix | 137-139 | 3 | |
| α-helix | 145-155 | 11 | |
| α-helix | 172-191 | 20 | |
| α-helix | 192-196 | 5 | |
| α-helix | 197-198 | 2 | |
| α-helix | 206-220 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H3-like centromeric protein CSE4, Protein SCM3, Histone H4 | A | protein | 235 | Saccharomyces cerevisiae | P02309 (AlphaFold model), P36012 (AlphaFold model), Q12334 (AlphaFold model) |
>2L5A_1 Histone H3-like centromeric protein CSE4, Protein SCM3, Histone H4 (chains A) MHHHHHHKKLLISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHT NLLALHAKRITIMKKDMQLARRIRGQFLVPRGSMERHKLADENMRKVWSNIISKYESIEE QGDLVDLKTGEIVEDNGHIKTLTANNSTKDKRTKYTSVLRDIIDISDEEDGDKGGVKRIS GLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
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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