Cryo-EM structure of the human SIN3B histone deacetylase core complex with SAHA at 2.8 Angstrom. Determined by electron microscopy at 2.8 Å resolution. Released 10 May 2023.
Explore 8BPC in 3D Show helices and sheets RCSB PDB PDBe
8BPC contains 55 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 | 428-429 | 2 | 1 |
| α-helix | 430-432 | 3 | |
| α-helix | 442-444 | 3 | |
| 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) |
>8BPC_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
>8BPC_2 Histone deacetylase 2 (chains B) MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKA TAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVA GAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHH GDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG GGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYM EKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEE FSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT KSEQLSNP
>8BPC_3 PHD finger protein 12 (chains C) MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCD SCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNG LVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQ NDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGS SKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDC LEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHK KHPP
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
| ZN | Zinc ion | Zn | 3 |
| SHH | Octanedioic acid hydroxyamide phenylamide | C14 H20 N2 O3 | 1 |
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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