8KD2: Rpd3S
Rpd3S in complex with 187bp nucleosome. Determined by electron microscopy at 3.02 Å resolution. Released 13 Sept 2023.
- Method
- Electron microscopy
- Resolution
- 3.02 Å
- Organisms
- Saccharomyces cerevisiae, Xenopus laevis, synthetic construct
- Chains
- 16
- Atoms
- 24,694
- Mol. weight
- 708.2 kDa
- Released
- 13 Sept 2023
Explore 8KD2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8KD2 contains 102 α-helices and 49 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: 18 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 21-24 | 4 | 1 |
| α-helix | 27-29 | 3 | |
| α-helix | 43-54 | 12 | |
| α-helix | 58-60 | 3 | |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 67-70 | 4 | |
| α-helix | 71-74 | 4 | |
| α-helix | 80-88 | 9 | |
| α-helix | 98-103 | 6 | |
| α-helix | 116-136 | 21 | |
| β-strand | 141-144 | 4 | 1 |
| β-strand | 153 | 1 | 2 |
| β-strand | 156 | 1 | 2 |
| α-helix | 165-172 | 8 | |
| β-strand | 180-184 | 5 | 1 |
| α-helix | 191-196 | 6 | |
| β-strand | 203-210 | 8 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 235-238 | 4 | 1 |
| α-helix | 244-261 | 18 | |
| β-strand | 266-270 | 5 | 1 |
| α-helix | 273-275 | 3 | |
| β-strand | 276 | 1 | 3 |
| β-strand | 286 | 1 | 3 |
| α-helix | 288-299 | 12 | |
| β-strand | 305-308 | 4 | 1 |
| α-helix | 315-329 | 15 | |
| β-strand | 337 | 1 | 4 |
| α-helix | 338-340 | 3 | |
| β-strand | 352 | 1 | 4 |
| α-helix | 356-358 | 3 | |
| α-helix | 366-380 | 15 | |
Chain B: 25 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 668-675 | 8 | |
| α-helix | 679-693 | 15 | |
| α-helix | 699-709 | 11 | |
| α-helix | 715-722 | 8 | |
| β-strand | 756-757 | 2 | 5 |
| β-strand | 782-783 | 2 | 5 |
| α-helix | 786-789 | 4 | |
| α-helix | 797-799 | 3 | |
| α-helix | 802-839 | 38 | |
| α-helix | 844-847 | 4 | |
| α-helix | 862-870 | 9 | |
| α-helix | 873-885 | 13 | |
| α-helix | 891-928 | 38 | |
| α-helix | 935-942 | 8 | |
| α-helix | 945-956 | 12 | |
| α-helix | 957-959 | 3 | |
| α-helix | 983-997 | 15 | |
| α-helix | 1004-1021 | 18 | |
| β-strand | 1136-1141 | 6 | 6 |
| α-helix | 1142-1163 | 22 | |
| α-helix | 1165-1173 | 9 | |
| α-helix | 1180-1182 | 3 | |
| α-helix | 1203-1216 | 14 | |
| α-helix | 1221-1232 | 12 | |
| α-helix | 1237-1239 | 3 | |
| α-helix | 1242-1258 | 17 | |
| α-helix | 1261-1273 | 13 | |
| α-helix | 1284-1291 | 8 | |
| β-strand | 1300-1305 | 6 | 6 |
| β-strand | 1313-1316 | 4 | 6 |
Chain D: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 226-236 | 11 | |
| α-helix | 237-241 | 5 | |
| β-strand | 244-246 | 3 | 7 |
| α-helix | 254-264 | 11 | |
| α-helix | 274-291 | 18 | |
| α-helix | 293-296 | 4 | |
| α-helix | 303-315 | 13 | |
| α-helix | 328-336 | 9 | |
| α-helix | 338-342 | 5 | |
| α-helix | 349-368 | 20 | |
| α-helix | 370-373 | 4 | |
| β-strand | 387-389 | 3 | 7 |
| α-helix | 390-391 | 2 | |
| α-helix | 392-398 | 7 | |
Chain E: 10 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 296-297 | 2 | |
| α-helix | 307-310 | 4 | |
| α-helix | 322-329 | 8 | |
| α-helix | 334-336 | 3 | |
| α-helix | 337-341 | 5 | |
| α-helix | 358-360 | 3 | |
| β-strand | 365 | 1 | 8 |
| β-strand | 373 | 1 | 8 |
| β-strand | 376 | 1 | 9 |
| α-helix | 401-406 | 6 | |
| α-helix | 431-433 | 3 | |
| β-strand | 437-439 | 3 | 10 |
| β-strand | 446-448 | 3 | 10 |
| β-strand | 462 | 1 | 9 |
| α-helix | 463-466 | 4 | |
| β-strand | 475 | 1 | 11 |
| β-strand | 491 | 1 | 11 |
| β-strand | 521-523 | 3 | 12 |
| β-strand | 541-543 | 3 | 12 |
| α-helix | 544-560 | 17 | |
Chain F: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 349-351 | 3 | |
| α-helix | 353-359 | 7 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 323-329 | 7 | |
Chain O: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-56 | 12 | |
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 13 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 14 |
| α-helix | 121-130 | 10 | |
Chain P: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 14 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 13 |
| α-helix | 83-92 | 10 | |
| β-strand | 96-98 | 3 | 15 |
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 | 1544 | 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 |
| 187bp DNA | X | DNA | 187 | synthetic construct | |
| 187bp DNA | Y | DNA | 187 | synthetic construct | |
Sequence of entity 1 (A), FASTA
>8KD2_1 Histone deacetylase RPD3 (chains A)
MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKK
MEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYC
SISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRV
LYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRD
GIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKS
FGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNM
FNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQY
ARDLHVEHDNEFY
Sequence of entity 2 (B), FASTA
>8KD2_2 Transcriptional regulatory protein SIN3 (chains B)
MHHHHHHHHSQVWHNSNSQSNDVATSNDATGSNERNEKEPSLQGNKPGFVQQQQRITLPS
LSALSTKEEDRRDSNGQQALTSHAAHILGYPPPHSNAMPSIATDSALKQPHEYHPRPKSS
SSSPSINASLMNAGPAPLPTVGAASFSLSRFDNPLPIKAPVHTEEPKSYNGLQEEEKATQ
RPQDCKEVPAGVQPADAPDPSSNHADANDDNNNNENSHDEDADYRPLNVKDALSYLEQVK
FQFSSRPDIYNLFLDIMKDFKSQAIDTPGVIERVSTLFRGYPILIQGFNTFLPQGYRIEC
SSNPDDPIRVTTPMGTTTVNNNISPSGRGTTDAQELGSFPESDGNGVQQPSNVPMVPSSV
YQSEQNQDQQQSLPLLATSSGLPSIQQPEMPAHRQIPQSQSLVPQEDAKKNVDVEFSQAI
SYVNKIKTRFADQPDIYKHFLEILQTYQREQKPINEVYAQVTHLFQNAPDLLEDFKKFLP
DSSASANQQVQHAQQHAQQQHEAQMHAQAQAQAQAQAQVEQQKQQQQFLYPASGYYGHPS
NRGIPQQNLPPIGSFSPPTNGSTVHEAYQDQQHMQPPHFMPLPSIVQHGPNMVHQGIANE
NPPLSDLRTSLTEQYAPSSIQHQQQHPQSISPIANTQYGDIPVRPEIDLDPSIVPVVPEP
TEPIENNISLNEEVTFFEKAKRYIGNKHLYTEFLKILNLYSQDILDLDDLVEKVDFYLGS
NKELFTWFKNFVGYQEKTKCIENIVHEKHRLDLDLCEAFGPSYKRLPKSDTFMPCSGRDD
MCWEVLNDEWVGHPVWASEDSGFIAHRKNQYEETLFKIEEERHEYDFYIESNLRTIQCLE
TIVNKIENMTENEKANFKLPPGLGHTSMTIYKKVIRKVYDKERGFEIIDALHEHPAVTAP
VVLKRLKQKDEEWRRAQREWNKVWRELEQKVFFKSLDHLGLTFKQADKKLLTTKQLISEI
SSIKVDQTNKKIHWLTPKPKSQLDFDFPDKNIFYDILCLADTFITHTTAYSNPDKERLKD
LLKYFISLFFSISFEKIEESLYSHKQNVSESSGSDDGSSIASRKRPYQQEMSLLDILHRS
RYQKLKRSNDEDGKVPQLSEPPEEEPNTIEEEELIDEEAKNPWLTGNLVEEANSQGIIQN
RSIFNLFANTNIYIFFRHWTTIYERLLEIKQMNERVTKEINTRSTVTFAKDLDLLSSQLS
EMGLDFVGEDAYKQVLRLSRRLINGDLEHQWFEESLRQAYNNKAFKLYTIDKVTQSLVKH
AHTLMTDAKTAEIMALFVKDRNASTTSAKDQIIYRLQVRSHMSNTENMFRIEFDKRTLHV
SIQYIALDDLTLKEPKADEDKWKYYVTSYALPHPTEGIPHEKLKIPFLERLIEFGQDIDG
TEVDEEFSPEGISVSTLKIKIQPITYQLHIENGSYDVFTRKATNKYPTIANDNTQKGMVS
QKKELISKFLDCAVGLRNNLDEAQKLSMQKKWENLKDSIAKTSAGNQGIESETEKGKITK
QEQSDNLDSSTASVLPASITTVPQDDNIETTGNTESSDKGAKIQ
Sequence of entity 3 (D, F), FASTA
>8KD2_3 Chromatin modification-related protein EAF3 (chains D, F)
MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQK
LGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKK
SLLEQQKKKKLSTSLGGPSNGGKRKGDSRSNASISKSTSQSFLTSSVSGRKSGRSSANSL
HPGSSLRSSSDQNGNDDRRRSSSLSPNMLHHIAGYPTPKISLQIPIKLKSVLVDDWEYVT
KDKKICRLPADVTVEMVLNKYEHEVSQELESPGSQSQLSEYCAGLKLYFDKCLGNMLLYR
LERLQYDELLKKSSKDQKPLVPIRIYGAIHLLRLISVLPELISSTTMDLQSCQLLIKQTE
DFLVWLLMHVDEYFNDKDPNRSDDALYVNTSSQYEGVALGM
Sequence of entity 4 (E, G), FASTA
>8KD2_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
>8KD2_5 Histone H3 (chains O, S)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 6 (P, T), FASTA
>8KD2_6 Histone H4 (chains P, T)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 7 (Q, U), FASTA
>8KD2_7 Histone H2A (chains Q, U)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 8 (R, V), FASTA
>8KD2_8 Histone H2B 1.1 (chains R, V)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 9 (X), FASTA
>8KD2_9 187bp DNA (chains X)
GCGGTGGCGGCCGCTCTAGAACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGA
GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA
GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCCAGGGCGGCCGCGTAT
AGGGTCC
Sequence of entity 10 (Y), FASTA
>8KD2_10 187bp DNA (chains Y)
GGACCCTATACGCGGCCGCCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAG
ACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGG
GGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTTCTAGAGCGGCCG
CCACCGC
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
- 8KD6 3.07 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class3
- 8KD7 3.09 Å, Rpd3S in complex with nucleosome with H3K36MLA modification and 167bp DNA
- 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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