Crystal structure of Nurf55 in complex with histone H3. Determined by X-ray diffraction at 2.55 Å resolution. Released 11 May 2011.
Explore 2YBA in 3D Show helices and sheets RCSB PDB PDBe
2YBA contains 17 α-helices and 60 β-strands across 4 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 | 12-35 | 24 | |
| β-strand | 36-43 | 8 | 1 |
| β-strand | 52-59 | 8 | 2 |
| β-strand | 65-73 | 9 | 2 |
| α-helix | 80 | 1 | |
| β-strand | 81-91 | 11 | 2 |
| β-strand | 119-127 | 9 | 2 |
| β-strand | 133-137 | 5 | 3 |
| β-strand | 140-147 | 8 | 3 |
| β-strand | 153-157 | 5 | 3 |
| α-helix | 158-160 | 3 | |
| α-helix | 165-166 | 2 | |
| β-strand | 175-178 | 4 | 3 |
| β-strand | 187-189 | 3 | 4 |
| β-strand | 196-200 | 5 | 4 |
| β-strand | 206-210 | 5 | 4 |
| α-helix | 214-215 | 2 | |
| β-strand | 216 | 1 | 3 |
| β-strand | 220-222 | 3 | 3 |
| β-strand | 225-227 | 3 | 4 |
| β-strand | 234-239 | 6 | 5 |
| β-strand | 246-251 | 6 | 5 |
| β-strand | 255-260 | 6 | 5 |
| β-strand | 271-274 | 4 | 5 |
| β-strand | 280-285 | 6 | 6 |
| β-strand | 292-297 | 6 | 6 |
| β-strand | 301-306 | 6 | 6 |
| β-strand | 315-318 | 4 | 6 |
| β-strand | 324-329 | 6 | 7 |
| β-strand | 336-341 | 6 | 7 |
| β-strand | 346-350 | 5 | 7 |
| α-helix | 351-353 | 3 | |
| α-helix | 360-363 | 4 | |
| β-strand | 370-374 | 5 | 7 |
| β-strand | 381-386 | 6 | 1 |
| β-strand | 393-398 | 6 | 1 |
| β-strand | 402-408 | 7 | 1 |
| α-helix | 410-413 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-35 | 24 | |
| β-strand | 36-43 | 8 | 8 |
| β-strand | 52-59 | 8 | 9 |
| β-strand | 65-73 | 9 | 9 |
| β-strand | 81-91 | 11 | 9 |
| β-strand | 119-127 | 9 | 9 |
| β-strand | 133-137 | 5 | 10 |
| β-strand | 140-147 | 8 | 10 |
| β-strand | 153-157 | 5 | 10 |
| α-helix | 158-160 | 3 | |
| α-helix | 165-166 | 2 | |
| β-strand | 175-178 | 4 | 10 |
| β-strand | 187-189 | 3 | 11 |
| β-strand | 196-200 | 5 | 11 |
| β-strand | 206-210 | 5 | 11 |
| α-helix | 214-215 | 2 | |
| β-strand | 216 | 1 | 10 |
| β-strand | 220-222 | 3 | 10 |
| β-strand | 225-227 | 3 | 11 |
| β-strand | 234-239 | 6 | 12 |
| β-strand | 246-251 | 6 | 12 |
| β-strand | 255-260 | 6 | 12 |
| β-strand | 271-274 | 4 | 12 |
| β-strand | 280-285 | 6 | 13 |
| β-strand | 292-297 | 6 | 13 |
| β-strand | 301-306 | 6 | 13 |
| β-strand | 315-318 | 4 | 13 |
| β-strand | 324-329 | 6 | 14 |
| β-strand | 336-341 | 6 | 14 |
| β-strand | 346-350 | 5 | 14 |
| α-helix | 351-353 | 3 | |
| α-helix | 360-363 | 4 | |
| β-strand | 370-374 | 5 | 14 |
| β-strand | 381-386 | 6 | 8 |
| β-strand | 393-398 | 6 | 8 |
| β-strand | 402-408 | 7 | 8 |
| α-helix | 410-413 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Probable histone-binding protein CAF1 | A, B | protein | 422 | DROSOPHILA MELANOGASTER | Q24572 (AlphaFold model) |
| Histone H3 | C, D | protein | 19 | DROSOPHILA MELANOGASTER | P02299 (AlphaFold model) |
>2YBA_1 PROBABLE HISTONE-BINDING PROTEIN CAF1 (chains A, B) GGGRMVDRSDNAAESFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPD VTKQDGKDYSVHRLILGTHTSDEQNHLLIASVQLPSEDAQFDGSHYDNEKGEFGGFGSVC GKIEIEIKINHEGEVNRARYMPQNACVIATKTPSSDVLVFDYTKHPSKPEPSGECQPDLR LRGHQKEGYGLSWNPNLNGYLLSASDDHTICLWDINATPKEHRVIDAKNIFTGHTAVVED VAWHLLHESLFGSVADDQKLMIWDTRNNNTSKPSHTVDAHTAEVNCLSFNPYSEFILATG SADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLHVWDLSKIGE EQSTEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWIICSVSEDNIMQVWQMAENVYNDE EP
>2YBA_2 HISTONE H3 (chains C, D) ARTKQTARKSTGGKAPRKQ
Histone Methylation by Prc2 is Inhibited by Active Chromatin Marks. Schmitges, F.W., Prusty, A.B., Faty, M. et al. Mol Cell (2011) 42:330. DOI 10.1016/J.MOLCEL.2011.03.025 · PubMed
Other PDB entries of the same protein (UniProt Q24572 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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