Cryo-EM structure of the human SIN3B full-length complex at 3.4 Angstrom resolution. Determined by electron microscopy at 3.4 Å resolution. Released 10 May 2023.
Explore 8C60 in 3D Show helices and sheets RCSB PDB PDBe
8C60 contains 70 α-helices and 27 β-strands across 4 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 | 305-318 | 14 | |
| α-helix | 321-333 | 13 | |
| α-helix | 334-338 | 5 | |
| α-helix | 341-352 | 12 | |
| α-helix | 356-366 | 11 | |
| β-strand | 396-397 | 2 | 1 |
| β-strand | 401-403 | 3 | 1 |
| α-helix | 404-405 | 2 | |
| α-helix | 410-412 | 3 | |
| α-helix | 418-423 | 6 | |
| β-strand | 428-430 | 3 | 1 |
| α-helix | 447-483 | 37 | |
| α-helix | 488-491 | 4 | |
| α-helix | 507-516 | 10 | |
| α-helix | 517-519 | 3 | |
| α-helix | 520-529 | 10 | |
| α-helix | 531-560 | 30 | |
| α-helix | 568-572 | 5 | |
| α-helix | 576-586 | 11 | |
| α-helix | 589-609 | 21 | |
| β-strand | 620-624 | 5 | 2 |
| α-helix | 628-641 | 14 | |
| α-helix | 649-657 | 9 | |
| α-helix | 658-662 | 5 | |
| α-helix | 663-666 | 4 | |
| β-strand | 739-745 | 7 | 2 |
| α-helix | 747-785 | 39 | |
| α-helix | 789-791 | 3 | |
| α-helix | 805-807 | 3 | |
| α-helix | 809-813 | 5 | |
| α-helix | 815-828 | 14 | |
| α-helix | 833-844 | 12 | |
| α-helix | 845-851 | 7 | |
| α-helix | 854-870 | 17 | |
| α-helix | 872-887 | 16 | |
| β-strand | 892-893 | 2 | 2 |
| α-helix | 897-912 | 16 | |
| β-strand | 921-928 | 8 | 2 |
| β-strand | 931-938 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-15 | 3 | 3 |
| α-helix | 20-22 | 3 | |
| α-helix | 34-45 | 12 | |
| β-strand | 54-55 | 2 | 3 |
| α-helix | 57-61 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 71-79 | 9 | |
| α-helix | 82-84 | 3 | |
| α-helix | 89-94 | 6 | |
| α-helix | 107-126 | 20 | |
| β-strand | 132-135 | 4 | 3 |
| β-strand | 149 | 1 | 4 |
| β-strand | 152 | 1 | 4 |
| α-helix | 156-164 | 9 | |
| β-strand | 171-175 | 5 | 3 |
| α-helix | 182-187 | 6 | |
| β-strand | 194-201 | 8 | 3 |
| α-helix | 218-220 | 3 | |
| β-strand | 224-229 | 6 | 3 |
| α-helix | 235-253 | 19 | |
| β-strand | 257-261 | 5 | 3 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 5 |
| β-strand | 277 | 1 | 5 |
| α-helix | 279-290 | 12 | |
| β-strand | 296-299 | 4 | 3 |
| α-helix | 306-320 | 15 | |
| β-strand | 328 | 1 | 6 |
| α-helix | 329-331 | 3 | |
| α-helix | 335-338 | 4 | |
| β-strand | 343 | 1 | 6 |
| α-helix | 347-349 | 3 | |
| α-helix | 357-372 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-28 | 8 | |
| β-strand | 68-70 | 3 | 7 |
| β-strand | 77-79 | 3 | 7 |
| α-helix | 86-88 | 3 | |
| α-helix | 100-111 | 12 | |
| α-helix | 207-219 | 13 | |
| α-helix | 229-232 | 4 | |
| β-strand | 274 | 1 | 8 |
| β-strand | 287-288 | 2 | 8 |
| β-strand | 295-296 | 2 | 8 |
| α-helix | 304-305 | 2 | |
| α-helix | 320-324 | 5 | |
| α-helix | 331-340 | 10 | |
| α-helix | 348-359 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 206-211 | 6 | |
| α-helix | 212-216 | 5 | |
| α-helix | 220-222 | 3 | |
| α-helix | 229-240 | 12 | |
| α-helix | 250-265 | 16 | |
| α-helix | 278-287 | 10 | |
| α-helix | 299-312 | 14 | |
| α-helix | 313-315 | 3 | |
| α-helix | 320-339 | 20 | |
| α-helix | 341-344 | 4 | |
| α-helix | 355-361 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 2 of Paired amphipathic helix protein Sin3b | A | protein | 1130 | Homo sapiens | O75182 (AlphaFold model) |
| Histone deacetylase 2 | B | protein | 488 | Homo sapiens | Q92769 (AlphaFold model) |
| PHD finger protein 12 | C | protein | 1004 | Homo sapiens | Q96QT6 (AlphaFold model) |
| Mortality factor 4-like protein 1 | D | protein | 362 | Homo sapiens | Q9UBU8 (AlphaFold model) |
>8C60_1 Isoform 2 of Paired amphipathic helix protein Sin3b (chains A) MAHAGGGSGGSGAGGPAGRGLSGARWGRSGSAGHEKLPVHVEDALTYLDQVKIRFGSDPA TYNGFLEIMKEFKSQSIDTPGVIRRVSQLFHEHPDLIVGFNAFLPLGYRIDIPKNGKLNI QSPLTSQENSHNHGDGAEDFKQQVPYKEDKPQVPLESDSVEFNNAISYVNKIKTRFLDHP EIYRSFLEILHTYQKEQLNTRGRPFRGMSEEEVFTEVANLFRGQEDLLSEFGQFLPEAKR SLFTGNGPCEMHSVQKNEHDKTPEHSRKRSRPSLLRPVSAPAKKKMKLRGTKDLSIAAVG KYGTLQEFSFFDKVRRVLKSQEVYENFLRCIALFNQELVSGSELLQLVSPFLGKFPELFA QFKSFLGVKELSFAPPMSDRSGDGISREIDYASCKRIGSSYRALPKTYQQPKCSGRTAIC KEVLNDTWVSFPSWSEDSTFVSSKKTPYEEQLHRCEDERFELDVVLETNLATIRVLESVQ KKLSRMAPEDQEKFRLDDSLGGTSEVIQRRAIYRIYGDKAPEIIESLKKNPVTAVPVVLK RLKAKEEEWREAQQGFNKIWREQYEKAYLKSLDHQAVNFKQNDTKALRSKSLLNEIESVY DEHQEQHSEGRSAPSSEPHLIFVYEDRQILEDAAALISYYVKRQPAIQKEDQGTIHQLLH QFVPSLFFSQQLDLGASEESADEDRDSPQGQTTDPSERKKPAPGPHSSPPEEKGAFGDAP ATEQPPLPPPAPHKPLDDVYSLFFANNNWYFFLRLHQTLCSRLLKIYRQAQKQLLEYRTE KEREKLLCEGRREKGSDPAMELRLKQPSEVELEEYYPAFLDMVRSLLEGSIDPTQYEDTL REMFTIHAYVGFTMDKLVQNIARQLHHLVSDDVCLKVVELYLNEKKRGAAGGNLSSRCVR AARETSYQWKAERCMADENCFKVMFLQRKGQVIMTIELLDTEEAQTEDPVEVQHLARYVE QYVGTEGASSSPTEGFLLKPVFLQRNLKKFRRRWQSEQARALRGEARSSWKRLVGVESAC DVDCRFKLSTHKMVFIVNSEDYMYRRGTLCRAKQVQPLVLLRHHQHFEEWHSRWLEDNVT VEAASLVQDWLMGEEDEDMVPCKTLCETVHVHGLPVTRYRVQYSRRPASP
>8C60_2 Histone deacetylase 2 (chains B) MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKA TAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVA GAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHH GDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG GGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYM EKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEE FSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT KSEQLSNP
>8C60_3 PHD finger protein 12 (chains C) MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCD SCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNG LVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQ NDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGS SKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDC LEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHK KHPPNRRVLQSVKRRSLKVPDAIKSQYQFPPPLIAPAAIRDGELICNGIPEESQMHLLNS EHLATQAEQQEWLCSVVALQCSILKHLSAKQMPSHWDSEQTEKADIKPVIVTDSSVTTSL QTADKTPTPSHYPLSCPSGISTQNSLSCSPPHQSPALEDIGCSSCAEKSKKTPCGTANGP VNTEVKANGPHLYSSPTDSTDPRRLPGANTPLPGLSHRQGWPRPLTPPAAGGLQNHTVGI IVKTENATGPSSCPQRSLVPVPSLPPSIPSSCASIENTSTLQRKTVQSQIGPPLTDSRPL GSPPNATRVLTPPQAAGDGILATTANQRFSSPAPSSDGKVSPGTLSIGSALTVPSFPANS TAMVDLTNSLRAFMDVNGEIEINMLDEKLIKFLALQRIHQLFPSRVQPSPGSVGTHQLAS GGHHIEVQRKEVQARAVFYPLLGLGGAVNMCYRTLYIGTGADMDVCLTNYGHCNYVSGKH ACIFYDENTKHYELLNYSEHGTTVDNVLYSCDFSEKTPPTPPSSIVAKVQSVIRRRRHQK QDEEPSEEAAMMSSQAQGPQRRPCNCKASSSSLIGGSGAGWEGTALLHHGSYIKLGCLQF VFSITEFATKQPKGDASLLQDGVLAEKLSLKPHQGPVLRSNSVP
>8C60_4 Mortality factor 4-like protein 1 (chains D) MAPKQDPKPKFQEGERVLCFHGPLLYEAKCVKVAIKDKQVKYFIHYSGWNKKSAVRPRRS EKSLKTHEDIVALFPVPEGAPSVHHPLLTSSWDEWVPESRVLKYVDTNLQKQRELQKANQ EQYAEGKMRGAAPGKKTSGLQQKNVEVKTKKNKQKTPGNGDGGSTSETPQPPRKKRARVD PTVENEETFMNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYK KSRGNTDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAP HLLRLFVRIGAMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRK AV
Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex. Wan, M.S.M., Muhammad, R., Koliopoulos, M.G. et al. Nat Commun (2023) 14:2556-2556. DOI 10.1038/s41467-023-38276-0 · PubMed
Other PDB entries of the same protein (UniProt O75182 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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