Cryo-EM structure of the human SIN3B histone deacetylase core complex at 2.8 Angstrom. Determined by electron microscopy at 2.8 Å resolution. Released 10 May 2023.
Explore 8BPB in 3D Show helices and sheets RCSB PDB PDBe
8BPB contains 53 α-helices and 25 β-strands across 3 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 | 322-333 | 12 | |
| α-helix | 334-338 | 5 | |
| α-helix | 341-348 | 8 | |
| 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 | 564-572 | 9 | |
| α-helix | 576-586 | 11 | |
| α-helix | 589-609 | 21 | |
| β-strand | 620-624 | 5 | 2 |
| α-helix | 627-642 | 16 | |
| 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 | 806-808 | 3 | |
| α-helix | 809-828 | 20 | |
| 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 | 897-914 | 18 | |
| 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 | 53-55 | 3 | 3 |
| α-helix | 57-61 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 71-79 | 9 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86-88 | 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 |
| β-strand | 267 | 1 | 5 |
| β-strand | 277 | 1 | 5 |
| α-helix | 279-291 | 13 | |
| 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 | 357-371 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-27 | 7 | |
| β-strand | 274 | 1 | 7 |
| β-strand | 286-288 | 3 | 7 |
| β-strand | 295-297 | 3 | 7 |
| α-helix | 304-305 | 2 | |
| α-helix | 320-323 | 4 | |
| α-helix | 331-339 | 9 | |
| α-helix | 348-359 | 12 |
| 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 | 364 | Homo sapiens | Q96QT6 (AlphaFold model) |
>8BPB_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
>8BPB_2 Histone deacetylase 2 (chains B) MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKA TAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVA GAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHH GDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG GGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYM EKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEE FSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT KSEQLSNP
>8BPB_3 PHD finger protein 12 (chains C) MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCD SCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNG LVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQ NDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGS SKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDC LEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHK KHPP
Water and common crystallization additives (ACT) are not listed.
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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