crystal structure of Arabidopsis thaliana EBS in complex with an H3K27me3 peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Jul 2018.
Explore 5Z8L in 3D Show helices and sheets RCSB PDB PDBe
5Z8L contains 10 α-helices and 15 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-19 | 3 | |
| β-strand | 22-23 | 2 | 1 |
| α-helix | 24 | 1 | |
| β-strand | 30-31 | 2 | 1 |
| β-strand | 36-39 | 4 | 2 |
| α-helix | 47-48 | 2 | |
| β-strand | 49-58 | 10 | 2 |
| β-strand | 64-72 | 9 | 2 |
| α-helix | 74-76 | 3 | |
| β-strand | 89-100 | 12 | 2 |
| α-helix | 101-103 | 3 | |
| β-strand | 104-112 | 9 | 2 |
| α-helix | 113-117 | 5 | |
| β-strand | 126-134 | 9 | 2 |
| β-strand | 139-141 | 3 | 2 |
| β-strand | 145-146 | 2 | 3 |
| β-strand | 148 | 1 | 4 |
| β-strand | 153 | 1 | 4 |
| β-strand | 162-163 | 2 | 5 |
| β-strand | 170-171 | 2 | 5 |
| α-helix | 173-176 | 4 | |
| α-helix | 180-185 | 6 | |
| α-helix | 211-213 | 3 | |
| β-strand | 218-219 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-29 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromatin remodeling protein EBS | A | protein | 234 | Arabidopsis thaliana | F4JL28 (AlphaFold model) |
| H3K27me3 peptide | P | protein | 16 | Arabidopsis thaliana | P59226 (AlphaFold model) |
>5Z8L_1 Chromatin remodeling protein EBS (chains A) MAKTRPGVASKIKTGRKELDSYTIKGTNKVVRAGDCVLMRPSDAGKPPYVARVEKIEADA RNNVKVHCRWYYRPEESLGGRRQFHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLE NVGAEDYYCRFEYKAATGAFTPDRVAVYCKCEMPYNPDDLMVQCEGCKDWYHPACVGMTI EEAKKLDHFVCAECSSDDDVAASQNGFTSSPADDVKVRLSLFSHLLYRCSITYL
>5Z8L_2 H3K27me3 peptide (chains P) LATKAARKSAPATGGV
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
EBS is a bivalent histone reader that regulates floral phase transition in Arabidopsis. Yang, Z., Qian, S., Scheid, R.N. et al. Nat Genet (2018) 50:1247-1253. DOI 10.1038/s41588-018-0187-8 · PubMed
Other PDB entries of the same protein (UniProt F4JL28 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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