9UUO: The NuA3 histone acetyltransferase complex
The NuA3 histone acetyltransferase complex. Determined by electron microscopy at 3.68 Å resolution. Released 10 Dec 2025.
- Method
- Electron microscopy
- Resolution
- 3.68 Å
- Organism
- Saccharomyces cerevisiae S288C
- Chains
- 5
- Atoms
- 11,004
- Mol. weight
- 250.04 kDa
- Ligands
- ZN
- Released
- 10 Dec 2025
Explore 9UUO in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9UUO contains 53 α-helices and 41 β-strands across 5 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.
Chain A: 22 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 108-111 | 4 | 1 |
| β-strand | 115-119 | 5 | 1 |
| α-helix | 122-126 | 5 | |
| α-helix | 128-138 | 11 | |
| α-helix | 139-141 | 3 | |
| α-helix | 154-165 | 12 | |
| α-helix | 190-192 | 3 | |
| α-helix | 195-198 | 4 | |
| α-helix | 203-206 | 4 | |
| α-helix | 215-232 | 18 | |
| α-helix | 233-237 | 5 | |
| β-strand | 275-276 | 2 | 2 |
| β-strand | 280-282 | 3 | 2 |
| α-helix | 292-295 | 4 | |
| β-strand | 301-302 | 2 | 2 |
| β-strand | 309-310 | 2 | 2 |
| α-helix | 313-322 | 10 | |
| β-strand | 331-336 | 6 | 3 |
| β-strand | 339-343 | 5 | 3 |
| α-helix | 350-360 | 11 | |
| β-strand | 379-386 | 8 | 3 |
| β-strand | 396-405 | 10 | 3 |
| β-strand | 418-421 | 4 | 3 |
| α-helix | 423-425 | 3 | |
| α-helix | 430-445 | 16 | |
| α-helix | 457-484 | 28 | |
| β-strand | 493-494 | 2 | 4 |
| β-strand | 496-497 | 2 | 5 |
| α-helix | 499-506 | 8 | |
| α-helix | 510-517 | 8 | |
| β-strand | 523-525 | 3 | 6 |
| β-strand | 526 | 1 | 7 |
| β-strand | 539-542 | 4 | 6 |
| α-helix | 546-557 | 12 | |
| β-strand | 584-586 | 3 | 8 |
| α-helix | 615-624 | 10 | |
| α-helix | 666-668 | 3 | |
| α-helix | 679-692 | 14 | |
| α-helix | 694-695 | 2 | |
| β-strand | 696-697 | 2 | 4 |
| β-strand | 707 | 1 | 7 |
Chain B: 19 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 31-32 | 2 | 5 |
| β-strand | 33-34 | 2 | 6 |
| β-strand | 73 | 1 | 9 |
| β-strand | 76 | 1 | 9 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-93 | 3 | 2 |
| α-helix | 114-119 | 6 | |
| α-helix | 145-147 | 3 | |
| α-helix | 162-174 | 13 | |
| α-helix | 176-178 | 3 | |
| α-helix | 189-201 | 13 | |
| α-helix | 209-228 | 20 | |
| α-helix | 235-251 | 17 | |
| β-strand | 281-282 | 2 | 10 |
| β-strand | 289-290 | 2 | 10 |
| α-helix | 292-295 | 4 | |
| β-strand | 299-301 | 3 | 8 |
| α-helix | 308-312 | 5 | |
| β-strand | 320 | 1 | 11 |
| β-strand | 323 | 1 | 11 |
| β-strand | 330-331 | 2 | 12 |
| β-strand | 332-333 | 2 | 13 |
| β-strand | 339-340 | 2 | 12 |
| α-helix | 341-346 | 6 | |
| β-strand | 351-352 | 2 | 13 |
| β-strand | 360-362 | 3 | 13 |
| α-helix | 369-373 | 5 | |
| β-strand | 376 | 1 | 14 |
| β-strand | 387-388 | 2 | 14 |
| β-strand | 397-398 | 2 | 14 |
| α-helix | 400-405 | 6 | |
| β-strand | 410-411 | 2 | 15 |
| α-helix | 417-420 | 4 | |
| β-strand | 432-433 | 2 | 15 |
| α-helix | 444-445 | 2 | |
| α-helix | 447-465 | 19 | |
| α-helix | 497-510 | 14 | |
| α-helix | 516-533 | 18 | |
| α-helix | 552-601 | 50 | |
Chain C: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-16 | 4 | |
| α-helix | 18 | 1 | |
| α-helix | 19-23 | 5 | |
| α-helix | 24-40 | 17 | |
| α-helix | 47-96 | 50 | |
| α-helix | 98-101 | 4 | |
Chain E: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 179-188 | 10 | |
| α-helix | 191-203 | 13 | |
| β-strand | 211-214 | 4 | 1 |
| β-strand | 219-223 | 5 | 1 |
| α-helix | 229-243 | 15 | |
Chain F: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-51 | 40 | |
| α-helix | 94-97 | 4 | |
| α-helix | 100-109 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone acetyltransferase SAS3 | A | protein | 831 | Saccharomyces cerevisiae S288C | P34218 (AlphaFold model) |
| NuA3 HAT complex component NTO1 | B | protein | 748 | Saccharomyces cerevisiae S288C | Q12311 (AlphaFold model) |
| Protein YNG1 | C | protein | 219 | Saccharomyces cerevisiae S288C | Q08465 (AlphaFold model) |
| Chromatin modification-related protein EAF6 | F | protein | 113 | Saccharomyces cerevisiae S288C | P47128 (AlphaFold model) |
| Transcription initiation factor TFIID subunit 14 | E | protein | 244 | Saccharomyces cerevisiae S288C | P35189 |
Sequence of entity 1 (A), FASTA
>9UUO_1 Histone acetyltransferase SAS3 (chains A)
MSLTANDESPKPKKNALLKNLEIDDLIHSQFVRSDTNGHRTTRRLFNSDASISHRIRGSV
RSDKGLNKIKKGLISQQSKLASENSSQNIVNRDNKMGAVSFPIIEPNIEVSEELKVRIKY
DSIKFFNFERLISKSSVIAPLVNKNITSSGPLIGFQRRVNRLKQTWDLATENMEYPYSSD
NTPFRDNDSWQWYVPYGGTIKKMKDFSTKRTLPTWEDKIKFLTFLENSKSATYINGNVSL
CNHNETDQENEDRKKRKGKVPRIKNKVWFSQIEYIVLRNYEIKPWYTSPFPEHINQNKMV
FICEFCLKYMTSRYTFYRHQLKCLTFKPPGNEIYRDGKLSVWEIDGRENVLYCQNLCLLA
KCFINSKTLYYDVEPFIFYILTEREDTENHPYQNAAKFHFVGYFSKEKFNSNDYNLSCIL
TLPIYQRKGYGQFLMEFSYLLSRKESKFGTPEKPLSDLGLLTYRTFWKIKCAEVLLKLRD
SARRRSNNKNEDTFQQVSLNDIAKLTGMIPTDVVFGLEQLQVLYRHKTRSLSSLDDFNYI
IKIDSWNRIENIYKTWSSKNYPRVKYDKLLWEPIILGPSFGINGMMNLEPTALADEALTN
ETMAPVISNNTHIENYNNSRAHNKRRRRRRRSSEHKTSKLHVNNIIEPEVPATDFFEDTV
SSLTEYMCDYKNTNNDRLIYQAEKRVLESIHDRKGIPRSKFSTETHWELCFTIKNSETPL
GNHAARRNDTGISSLEQDEVENDVDTELYVGENAKEDEDEDEDFTLDDDIEDEQISEEND
EEEDTYEEDSDDDEDGKRKGQEQDENDIESHIRKERVRKRRKITLIEDDEE
Sequence of entity 2 (B), FASTA
>9UUO_2 NuA3 HAT complex component NTO1 (chains B)
MNRGSLDDGPKLREEKHFQDFYPDLNADTLLPFIVPLVETKDNSTDTDSDDISNRNNREI
GSVKSVQTKELIFKGRVTTEPLVLKKNEVEFQKCKITTNELKGKKNPYCVRFNESFISRY
YHINKVRNRKSYKQQQKEFDGVEAPYFTKFSSKEAPNITISTSTKSAIQKFASISPNLVN
FKPQYDMDEQDELYLHYLNKRYFKDQMSHEIFEILMTTLETEWFHIEKHIPSTNSLIARH
NILRDCKNYELYGSDDGTGLSMDQACAVCLGTDSDNLNTIVFCDGCDIAVHQECYGIIFI
PEGKWLCRRCMISKNNFATCLMCPSHTGAFKQTDTGSWVHNICALWLPELYFSNLHYMEP
IEGVQNVSVSRWKLNCYICKKKMGACIQCFQRNCFTAYHVTCARRAGLYMSKGKCTIQEL
ASNQFSQKYSVESFCHKHAPRGWQTSIEGINKARKYFSLLSTLQTETPQHNEANDRTNSK
FNKTIWKTPNQTPVAPHVFAEILQKVVDFFGLANPPAGAFDICKYWSMKRELTGGTPLTA
CFENNSLGSLTEEQVQTRIDFANDQLEDLYRLKELTTLVKKRTQASNSLSRSRKKVFDIV
KSPQKYLLKINVLDIFIKSEQFKALERLVTEPKLLVILEKCKHCDFDTVQIFKEEIMHFF
EVLETLPGASRILQTVSSKAKEQVTNLIGLIEHVDIKKLLSRDFIINDDKIEERPWSGPV
IMEEEGLSDAEELSAGEHRMLKLILNSG
Sequence of entity 3 (C), FASTA
>9UUO_3 Protein YNG1 (chains C)
MEHLANENSDSDIRYSFLSTLDHLPCELIRSLRLMQTIDLFKNEEDEPGMERACRDLLLV
ATYINDLVDDQIHFLKQHKKELEIQKSVTKNFNSSLENIKSKLTLEEPGAYKEPKLLLKI
NLKKAKSRERKESITSPTIGINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEW
FHYGCVGLKQAPKGKWYCSKDCKEIANQRSKSKRQKRRK
Sequence of entity 4 (F), FASTA
>9UUO_4 Chromatin modification-related protein EAF6 (chains F)
MTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKETEYFSHNSNNNHSGHGGAHG
SKSHYSGNIIKGFDTFSKSHHSHADSAFNNNDRIFSLSSATYVKQQHGQSQND
Sequence of entity 5 (E), FASTA
>9UUO_5 Transcription initiation factor TFIID subunit 14 (chains E)
MVATVKRTIRIKTQQHILPEVPPVENFPVRQWSIEIVLLDDEGKEIPATIFDKVIYHLHP
TFANPNRTFTDPPFRIEEQGWGGFPLDISVFLLEKAGERKIPHDLNFLQESYEVEHVIQI
PLNKPLLTEELAKSGSTEETTANTGTIGKRRTTTNTTAEPKAKRAKTGSASTVKGSVDLE
KLAFGLTKLNEDDLVGVVQMVTDNKTPEMNVTNNVEEGEFIIDLYSLPEGLLKSLWDYVK
KNTE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 6 |
Primary citation
Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex. Shi, W., Zhao, L., Wang, Y. et al. Nat Commun (2025) 17:342-342. DOI 10.1038/s41467-025-67049-0 · PubMed
Other PDB entries of the same protein (UniProt P34218 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9VKW 3.13 Å, Cryo-EM structure of the NuA3 complex bound to Ace-coenzyme A
- 9UUS 3.2 Å, The NuA3 histone acetyltransferase complex bound to acetyl-CoA and H3 tail
Browse structure collections
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