8KD7: Rpd3S
Rpd3S in complex with nucleosome with H3K36MLA modification and 167bp DNA. Determined by electron microscopy at 3.09 Å resolution. Released 13 Sept 2023.
- Method
- Electron microscopy
- Resolution
- 3.09 Å
- Organisms
- Saccharomyces cerevisiae, Xenopus laevis, synthetic construct
- Chains
- 16
- Atoms
- 24,894
- Mol. weight
- 677.29 kDa
- Released
- 13 Sept 2023
Explore 8KD7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8KD7 contains 102 α-helices and 50 β-strands across 14 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: 16 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 21-24 | 4 | 1 |
| α-helix | 27-29 | 3 | |
| α-helix | 43-53 | 11 | |
| α-helix | 57-59 | 3 | |
| β-strand | 62-64 | 3 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 80-86 | 7 | |
| α-helix | 98-103 | 6 | |
| α-helix | 116-136 | 21 | |
| β-strand | 141-144 | 4 | 1 |
| α-helix | 167-173 | 7 | |
| β-strand | 180-185 | 6 | 1 |
| α-helix | 192-196 | 5 | |
| β-strand | 203-210 | 8 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 236-238 | 3 | 1 |
| α-helix | 244-260 | 17 | |
| β-strand | 267 | 1 | 1 |
| β-strand | 270 | 1 | 1 |
| β-strand | 276 | 1 | 2 |
| β-strand | 286 | 1 | 2 |
| α-helix | 288-299 | 12 | |
| β-strand | 305-308 | 4 | 1 |
| α-helix | 315-328 | 14 | |
| α-helix | 338-340 | 3 | |
| α-helix | 355-358 | 4 | |
| α-helix | 366-379 | 14 | |
| β-strand | 415 | 1 | 1 |
Chain B: 26 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 666-676 | 11 | |
| α-helix | 679-693 | 15 | |
| α-helix | 699-709 | 11 | |
| α-helix | 715-721 | 7 | |
| β-strand | 756-757 | 2 | 3 |
| α-helix | 758-759 | 2 | |
| α-helix | 774-777 | 4 | |
| β-strand | 782-783 | 2 | 3 |
| α-helix | 786-790 | 5 | |
| α-helix | 802-839 | 38 | |
| α-helix | 844-847 | 4 | |
| α-helix | 862-870 | 9 | |
| α-helix | 875-885 | 11 | |
| α-helix | 891-926 | 36 | |
| α-helix | 935-938 | 4 | |
| α-helix | 945-960 | 16 | |
| β-strand | 977 | 1 | 4 |
| α-helix | 984-998 | 15 | |
| α-helix | 1004-1021 | 18 | |
| α-helix | 1028-1030 | 3 | |
| β-strand | 1136-1140 | 5 | 4 |
| α-helix | 1142-1163 | 22 | |
| α-helix | 1165-1171 | 7 | |
| α-helix | 1203-1216 | 14 | |
| α-helix | 1221-1231 | 11 | |
| α-helix | 1238-1241 | 4 | |
| α-helix | 1242-1254 | 13 | |
| α-helix | 1260-1271 | 12 | |
| α-helix | 1283-1291 | 9 | |
| β-strand | 1301-1306 | 6 | 4 |
| α-helix | 1308-1310 | 3 | |
| β-strand | 1311-1315 | 5 | 4 |
Chain D: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 226-240 | 15 | |
| β-strand | 244-246 | 3 | 5 |
| α-helix | 255-264 | 10 | |
| α-helix | 274-292 | 19 | |
| α-helix | 304-313 | 10 | |
| α-helix | 328-337 | 10 | |
| α-helix | 349-368 | 20 | |
| β-strand | 387-389 | 3 | 5 |
| α-helix | 392-398 | 7 | |
Chain E: 12 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 53-56 | 4 | |
| β-strand | 272-274 | 3 | 6 |
| β-strand | 281-283 | 3 | 6 |
| α-helix | 296-297 | 2 | |
| α-helix | 304-308 | 5 | |
| α-helix | 309-313 | 5 | |
| α-helix | 322-324 | 3 | |
| α-helix | 327-329 | 3 | |
| α-helix | 343-345 | 3 | |
| α-helix | 355-360 | 6 | |
| β-strand | 365-366 | 2 | 7 |
| β-strand | 372-373 | 2 | 7 |
| β-strand | 376 | 1 | 8 |
| α-helix | 413-417 | 5 | |
| α-helix | 431-433 | 3 | |
| β-strand | 437-438 | 2 | 9 |
| β-strand | 447-448 | 2 | 9 |
| β-strand | 462 | 1 | 8 |
| α-helix | 500-502 | 3 | |
| β-strand | 520-522 | 3 | 10 |
| β-strand | 540-542 | 3 | 10 |
| α-helix | 544-558 | 15 | |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 276-289 | 14 | |
| α-helix | 333-337 | 5 | |
| α-helix | 338-340 | 3 | |
| α-helix | 349-363 | 15 | |
Chain G: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 321-326 | 6 | |
| α-helix | 331-333 | 3 | |
| α-helix | 545-562 | 18 | |
Chain O: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-54 | 10 | |
| α-helix | 64-73 | 10 | |
| β-strand | 83-84 | 2 | 11 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 12 |
| α-helix | 121-131 | 11 | |
Chain P: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 12 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 11 |
| α-helix | 83-92 | 10 | |
| β-strand | 96-98 | 3 | 13 |
6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone deacetylase RPD3 | A | protein | 433 | Saccharomyces cerevisiae | P32561 (AlphaFold model) |
| Transcriptional regulatory protein SIN3 | B | protein | 1371 | Saccharomyces cerevisiae | P22579 (AlphaFold model) |
| Chromatin modification-related protein EAF3 | D, F | protein | 401 | Saccharomyces cerevisiae | Q12432 (AlphaFold model) |
| Transcriptional regulatory protein RCO1 | E, G | protein | 733 | Saccharomyces cerevisiae | Q04779 (AlphaFold model) |
| Histone H3 | O, S | protein | 135 | Xenopus laevis | P84233 |
| Histone H4 | P, T | protein | 102 | Xenopus laevis | P62799 |
| Histone H2A | Q, U | protein | 129 | Xenopus laevis | P06897 |
| Histone H2B 1.1 | R, V | protein | 122 | Xenopus laevis | P02281 |
| 167bp DNA | X | DNA | 167 | synthetic construct | |
| 167bp DNA | Y | DNA | 167 | synthetic construct | |
Sequence of entity 1 (A), FASTA
>8KD7_1 Histone deacetylase RPD3 (chains A)
MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKK
MEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYC
SISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRV
LYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRD
GIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKS
FGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNM
FNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQY
ARDLHVEHDNEFY
Sequence of entity 2 (B), FASTA
>8KD7_2 Transcriptional regulatory protein SIN3 (chains B)
MHHHHHHHHPQLAMWSHPQFEKGGGSGGGSGGGSWSHPQFEKENLYFQSDYRPLNVKDAL
SYLEQVKFQFSSRPDIYNLFLDIMKDFKSQAIDTPGVIERVSTLFRGYPILIQGFNTFLP
QGYRIECSSNPDDPIRVTTPMGTTTVNNNISPSGRGTTDAQELGSFPESDGNGVQQPSNV
PMVPSSVYQSEQNQDQQQSLPLLATSSGLPSIQQPEMPAHRQIPQSQSLVPQEDAKKNVD
VEFSQAISYVNKIKTRFADQPDIYKHFLEILQTYQREQKPINEVYAQVTHLFQNAPDLLE
DFKKFLPDSSASANQQVQHAQQHAQQQHEAQMHAQAQAQAQAQAQVEQQKQQQQFLYPAS
GYYGHPSNRGIPQQNLPPIGSFSPPTNGSTVHEAYQDQQHMQPPHFMPLPSIVQHGPNMV
HQGIANENPPLSDLRTSLTEQYAPSSIQHQQQHPQSISPIANTQYGDIPVRPEIDLDPSI
VPVVPEPTEPIENNISLNEEVTFFEKAKRYIGNKHLYTEFLKILNLYSQDILDLDDLVEK
VDFYLGSNKELFTWFKNFVGYQEKTKCIENIVHEKHRLDLDLCEAFGPSYKRLPKSDTFM
PCSGRDDMCWEVLNDEWVGHPVWASEDSGFIAHRKNQYEETLFKIEEERHEYDFYIESNL
RTIQCLETIVNKIENMTENEKANFKLPPGLGHTSMTIYKKVIRKVYDKERGFEIIDALHE
HPAVTAPVVLKRLKQKDEEWRRAQREWNKVWRELEQKVFFKSLDHLGLTFKQADKKLLTT
KQLISEISSIKVDQTNKKIHWLTPKPKSQLDFDFPDKNIFYDILCLADTFITHTTAYSNP
DKERLKDLLKYFISLFFSISFEKIEESLYSHKQNVSESSGSDDGSSIASRKRPYQQEMSL
LDILHRSRYQKLKRSNDEDGKVPQLSEPPEEEPNTIEEEELIDEEAKNPWLTGNLVEEAN
SQGIIQNRSIFNLFANTNIYIFFRHWTTIYERLLEIKQMNERVTKEINTRSTVTFAKDLD
LLSSQLSEMGLDFVGEDAYKQVLRLSRRLINGDLEHQWFEESLRQAYNNKAFKLYTIDKV
TQSLVKHAHTLMTDAKTAEIMALFVKDRNASTTSAKDQIIYRLQVRSHMSNTENMFRIEF
DKRTLHVSIQYIALDDLTLKEPKADEDKWKYYVTSYALPHPTEGIPHEKLKIPFLERLIE
FGQDIDGTEVDEEFSPEGISVSTLKIKIQPITYQLHIENGSYDVFTRKATNKYPTIANDN
TQKGMVSQKKELISKFLDCAVGLRNNLDEAQKLSMQKKWENLKDSIAKTSAGNQGIESET
EKGKITKQEQSDNLDSSTASVLPASITTVPQDDNIETTGNTESSDKGAKIQ
Sequence of entity 3 (D, F), FASTA
>8KD7_3 Chromatin modification-related protein EAF3 (chains D, F)
MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQK
LGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKK
SLLEQQKKKKLSTSLGGPSNGGKRKGDSRSNASISKSTSQSFLTSSVSGRKSGRSSANSL
HPGSSLRSSSDQNGNDDRRRSSSLSPNMLHHIAGYPTPKISLQIPIKLKSVLVDDWEYVT
KDKKICRLPADVTVEMVLNKYEHEVSQELESPGSQSQLSEYCAGLKLYFDKCLGNMLLYR
LERLQYDELLKKSSKDQKPLVPIRIYGAIHLLRLISVLPELISSTTMDLQSCQLLIKQTE
DFLVWLLMHVDEYFNDKDPNRSDDALYVNTSSQYEGVALGM
Sequence of entity 4 (E, G), FASTA
>8KD7_4 Transcriptional regulatory protein RCO1 (chains E, G)
MDTSKKDTTRSPSHSNSSSPSSSSLSSSSSKEKKRPKRLSSQNVNYDLKRRKIITSEGIE
RSFKNEHSNLAVEDNIPEEEPKELLEKDSKGNIIKLNEPSTISEDSKVSVTGLPLNKGPS
EKIKRESLWNYRKNLGGQSNNSEMTLVPSKRFTQVPKNFQDLNRNDLKTFLTENMTEESN
IRSTIGWNGDIINRTRDREPESDRDNKKLSNIRTKIILSTNATYDSKSKLFGQNSIKSTS
NASEKIFRDKNNSTIDFENEDFCSACNQSGSFLCCDTCPKSFHFLCLDPPIDPNNLPKGD
WHCNECKFKIFINNSMATLKKIESNFIKQNNNVKIFAKLLFNIDSHNPKQFQLPNYIKET
FPAVKTGSRGQYSDENDKIPLTDRQLFNTSYGQSITKLDSYNPDTHIDSNSGKFLICYKC
NQTRLGSWSHPENSRLIMTCDYCQTPWHLDCVPRASFKNLGSKWKCPLHSPTKVYKKIHH
CQEDNSVNYKVWKKQRLINKKNQLYYEPLQKIGYQNNGNIQIIPTTSHTDYDFNQDFKIT
QIDENSIKYDFFDKIYKSKMVQKRKLFQFQESLIDKLVSNGSQNGNSEDNMVKDIASLIY
FQVSNNDKSSNNKSASKSNNLRKLWDLKELTNVVVPNELDSIQFNDFSSDEIKHLLYLKK
IIESKPKEELLKFLNIENPENQSEMHHHHHHHHPQLAMWSHPQFEKGGGSGGGSGGGSWS
HPQFEKENLYFQS
Sequence of entity 5 (O, S), FASTA
>8KD7_5 Histone H3 (chains O, S)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 6 (P, T), FASTA
>8KD7_6 Histone H4 (chains P, T)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 7 (Q, U), FASTA
>8KD7_7 Histone H2A (chains Q, U)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 8 (R, V), FASTA
>8KD7_8 Histone H2B 1.1 (chains R, V)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 9 (X), FASTA
>8KD7_9 167bp DNA (chains X)
GCGGTGGCGGCCGCTCTAGAACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGA
GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA
GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCCAG
Sequence of entity 10 (Y), FASTA
>8KD7_10 167bp DNA (chains Y)
CTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAA
ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA
GGCACGTGTCAGATATATACATCCTGTTCTAGAGCGGCCGCCACCGC
Primary citation
Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex. Dong, S., Li, H., Wang, M. et al. Cell Res (2023) 33:790-801. DOI 10.1038/s41422-023-00869-1 · PubMed
Other PDB entries of the same protein (UniProt P32561 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8HPO 2.6 Å, Cryo-EM structure of a SIN3/HDAC complex from budding yeast
- 8TOF 2.8 Å, Rpd3S bound to an H3K36Cme3 modified nucleosome
- 8KD3 2.9 Å, Rpd3S in complex with nucleosome with H3K36MLA modification, H3K9Q mutation and 187bp DNA
- 8KD5 2.9 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class2
- 8KD4 2.93 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class1
- 8HXX 3.0 Å, Cryo-EM structure of the histone deacetylase complex Rpd3S
- 9V2V 3.0 Å, Cryo-EM structure of the histone deacetylase complex Rpd3L in complex with mono-nucleosome
- 8KD2 3.02 Å, Rpd3S in complex with 187bp nucleosome
- 8KD6 3.07 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class3
- 8HXY 3.1 Å, Cryo-EM structure of the histone deacetylase complex Rpd3S in complex with nucleosome
- 8HY0 3.1 Å, Composite cryo-EM structure of the histone deacetylase complex Rpd3S in complex with…
- 7YI0 3.2 Å, Cryo-EM structure of Rpd3S complex
Browse structure collections
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