Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Sept 2008.
Explore 2ZFN in 3D Show helices and sheets RCSB PDB PDBe
2ZFN contains 18 α-helices and 24 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 | 3-10 | 8 | |
| β-strand | 12 | 1 | 1 |
| β-strand | 16-23 | 8 | 2 |
| α-helix | 24-26 | 3 | |
| β-strand | 27-29 | 3 | 2 |
| β-strand | 33 | 1 | 3 |
| α-helix | 34-36 | 3 | |
| β-strand | 45-57 | 13 | 2 |
| β-strand | 60-73 | 14 | 2 |
| β-strand | 79-90 | 12 | 2 |
| α-helix | 100-112 | 13 | |
| β-strand | 114 | 1 | 4 |
| α-helix | 117-120 | 4 | |
| β-strand | 123 | 1 | 5 |
| β-strand | 124 | 1 | 2 |
| α-helix | 132-134 | 3 | |
| α-helix | 135-137 | 3 | |
| β-strand | 177 | 1 | 5 |
| β-strand | 186-193 | 8 | 2 |
| α-helix | 204-206 | 3 | |
| α-helix | 215-233 | 19 | |
| β-strand | 234 | 1 | 6 |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 249-256 | 8 | |
| β-strand | 264-266 | 3 | 2 |
| β-strand | 277 | 1 | 7 |
| α-helix | 278-280 | 3 | |
| β-strand | 283 | 1 | 3 |
| α-helix | 289-299 | 11 | |
| β-strand | 307 | 1 | 7 |
| α-helix | 308-314 | 7 | |
| α-helix | 315-319 | 5 | |
| α-helix | 320-323 | 4 | |
| β-strand | 328-334 | 7 | 2 |
| β-strand | 336 | 1 | 6 |
| β-strand | 342 | 1 | 4 |
| β-strand | 350 | 1 | 2 |
| α-helix | 355-366 | 12 | |
| α-helix | 373-391 | 19 | |
| α-helix | 394-395 | 2 | |
| β-strand | 396-399 | 4 | 2 |
| β-strand | 402 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulator of Ty1 transposition protein 109 | A | protein | 460 | Saccharomyces cerevisiae | Q07794 (AlphaFold model) |
>2ZFN_1 Regulator of Ty1 transposition protein 109 (chains A) MGSSHHHHHHSSGLVPRGSHMAAMMSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPN KDDKRVPKSTIKTQHFFSLFHQGKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNT RVSVRDITKIILEFILSIDPNYYLQKVKPAIRSYKKISPELISAASTPARTLRILARRLK QSGSTVLKEIESPRFQQDLYLSFTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGE ELMKWWGFILDRLLIECFQNDTQAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENS LAVYNIPLFPDDPKARFIHQLAEEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYS LATPSLFPSSADVIVPKSRKQFRAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQ SLTGKREHRERNQPVPASNINTLAITMLKPRKKAKALPKT
| ID | Name | Formula | Copies |
|---|---|---|---|
| ACO | Acetyl coenzyme *a | C23 H38 N7 O17 P3 S | 1 |
Water and common crystallization additives (GOL) are not listed.
Structural insights into histone h3 lysine 56 acetylation by rtt109. Lin, C., Yuan, Y.A. Structure (2008) 16:1503-1510. DOI 10.1016/j.str.2008.07.006 · PubMed
Other PDB entries of the same protein (UniProt Q07794 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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