Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. Determined by X-ray diffraction at 3.3 Å resolution. Released 2 Feb 2011.
Explore 3Q35 in 3D Show helices and sheets RCSB PDB PDBe
3Q35 contains 27 α-helices and 26 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 | 3-8 | 6 | |
| β-strand | 12 | 1 | 1 |
| β-strand | 16-23 | 8 | 2 |
| β-strand | 27-29 | 3 | 2 |
| β-strand | 33 | 1 | 3 |
| α-helix | 34-36 | 3 | |
| β-strand | 45-56 | 12 | 2 |
| β-strand | 61-73 | 13 | 2 |
| β-strand | 79-90 | 12 | 2 |
| α-helix | 100-113 | 14 | |
| α-helix | 118-120 | 3 | |
| β-strand | 123 | 1 | 4 |
| β-strand | 124 | 1 | 2 |
| α-helix | 144-157 | 14 | |
| β-strand | 177 | 1 | 4 |
| β-strand | 186-193 | 8 | 2 |
| α-helix | 204-206 | 3 | |
| α-helix | 215-232 | 18 | |
| β-strand | 234 | 1 | 5 |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 249-256 | 8 | |
| β-strand | 265-266 | 2 | 2 |
| α-helix | 278-280 | 3 | |
| β-strand | 283 | 1 | 3 |
| α-helix | 289-299 | 11 | |
| α-helix | 308-316 | 9 | |
| β-strand | 328-334 | 7 | 2 |
| β-strand | 336 | 1 | 5 |
| α-helix | 339-340 | 2 | |
| β-strand | 350 | 1 | 2 |
| α-helix | 355-366 | 12 | |
| α-helix | 373-391 | 19 | |
| β-strand | 396-399 | 4 | 2 |
| β-strand | 402 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-51 | 42 | |
| α-helix | 57-64 | 8 | |
| α-helix | 67-70 | 4 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-80 | 4 | |
| β-strand | 83-90 | 8 | 6 |
| α-helix | 91-93 | 3 | |
| β-strand | 103-109 | 7 | 6 |
| β-strand | 112 | 1 | 7 |
| β-strand | 116 | 1 | 7 |
| β-strand | 119-128 | 10 | 6 |
| β-strand | 138-141 | 4 | 6 |
| α-helix | 151-153 | 3 | |
| α-helix | 157-159 | 3 | |
| α-helix | 166-175 | 10 | |
| α-helix | 180-182 | 3 | |
| α-helix | 197-203 | 7 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-219 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase | A | protein | 438 | Saccharomyces cerevisiae | Q07794 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 75 | B | protein | 232 | Saccharomyces cerevisiae | P53853 (AlphaFold model) |
>3Q35_1 Histone acetyltransferase (chains A) GSMSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQHFFSLFHQ GKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSVRDITKIILEFILSIDPNY YLQKVKPAIRSYKKISPELISAASTPARTLRILARRLKQSGSTVLKEIESPRFQQDLYLS FTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGEELMKWWGFILDRLLIECFQNDT QAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENSLAVYNIPLFPDDPKARFIHQLA EEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSADVIVPKSRKQF RAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREHRERNQPVPASNINT LAITMLKPRKKAKALPKT
>3Q35_2 Vacuolar protein sorting-associated protein 75 (chains B) MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKI VLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQ VTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIF GWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ACO | Acetyl coenzyme *a | C23 H38 N7 O17 P3 S | 1 |
Water and common crystallization additives (EDO) are not listed.
Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Tang, Y., Holbert, M.A., Delgoshaie, N. et al. Structure (2011) 19:221-231. DOI 10.1016/j.str.2010.12.012 · 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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