Potent, selective and CNS-penetrant tetrasubstituted cyclopropane class IIa histone deacetylase (HDAC) inhibitors. Determined by X-ray diffraction at 2.65 Å resolution. Released 10 Feb 2016.
Explore 5A2S in 3D Show helices and sheets RCSB PDB PDBe
5A2S contains 50 α-helices and 30 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 654-657 | 4 | 1 |
| α-helix | 660-664 | 5 | |
| α-helix | 672-674 | 3 | |
| α-helix | 680-691 | 12 | |
| α-helix | 695-697 | 3 | |
| β-strand | 699-701 | 3 | 1 |
| α-helix | 702-703 | 2 | |
| α-helix | 705-707 | 3 | |
| α-helix | 708-711 | 4 | |
| α-helix | 717-724 | 8 | |
| α-helix | 727-733 | 7 | |
| α-helix | 742-744 | 3 | |
| β-strand | 747-748 | 2 | 2 |
| β-strand | 754-755 | 2 | 2 |
| β-strand | 761 | 1 | 2 |
| α-helix | 767-786 | 20 | |
| β-strand | 792-795 | 4 | 1 |
| β-strand | 810 | 1 | 3 |
| β-strand | 813 | 1 | 3 |
| α-helix | 817-829 | 13 | |
| β-strand | 834-838 | 5 | 1 |
| α-helix | 845-851 | 7 | |
| β-strand | 857-864 | 8 | 1 |
| α-helix | 866-868 | 3 | |
| α-helix | 883-885 | 3 | |
| β-strand | 889-894 | 6 | 1 |
| α-helix | 904-910 | 7 | |
| α-helix | 911-915 | 5 | |
| α-helix | 916-922 | 7 | |
| β-strand | 926-931 | 6 | 1 |
| β-strand | 936 | 1 | 4 |
| β-strand | 948 | 1 | 4 |
| α-helix | 952-960 | 9 | |
| α-helix | 964-966 | 3 | |
| β-strand | 968-972 | 5 | 1 |
| α-helix | 978-992 | 15 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1002-1006 | 5 | |
| α-helix | 1007-1010 | 4 | |
| α-helix | 1011-1023 | 13 | |
| α-helix | 1024-1026 | 3 | |
| α-helix | 1029-1031 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 655-657 | 3 | 5 |
| α-helix | 660-664 | 5 | |
| α-helix | 680-690 | 11 | |
| α-helix | 695-697 | 3 | |
| β-strand | 699-700 | 2 | 5 |
| α-helix | 705-707 | 3 | |
| α-helix | 708-711 | 4 | |
| α-helix | 717-722 | 6 | |
| α-helix | 727-733 | 7 | |
| β-strand | 747-748 | 2 | 6 |
| β-strand | 754-755 | 2 | 6 |
| β-strand | 761 | 1 | 6 |
| α-helix | 767-786 | 20 | |
| β-strand | 793-795 | 3 | 5 |
| β-strand | 810 | 1 | 7 |
| β-strand | 813 | 1 | 7 |
| α-helix | 817-829 | 13 | |
| β-strand | 834-838 | 5 | 5 |
| α-helix | 845-851 | 7 | |
| β-strand | 857-864 | 8 | 5 |
| α-helix | 883-885 | 3 | |
| β-strand | 889-894 | 6 | 5 |
| α-helix | 901-902 | 2 | |
| α-helix | 904-910 | 7 | |
| α-helix | 911-915 | 5 | |
| α-helix | 916-922 | 7 | |
| β-strand | 926-931 | 6 | 5 |
| β-strand | 936 | 1 | 8 |
| β-strand | 948 | 1 | 8 |
| α-helix | 950-960 | 11 | |
| α-helix | 964-966 | 3 | |
| β-strand | 968-972 | 5 | 5 |
| α-helix | 978-992 | 15 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1002-1005 | 4 | |
| α-helix | 1008-1010 | 3 | |
| α-helix | 1011-1024 | 14 | |
| α-helix | 1029-1031 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone deacetylase 4 | A, B | protein | 395 | HOMO SAPIENS | P56524 (AlphaFold model) |
>5A2S_1 HISTONE DEACETYLASE 4 (chains A, B) MGSTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGR KATLEELQTVHSEAHTLLYGTNPANRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNE VHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKL LQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGP GVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLG GYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKV LQQRPNANAVRSMEKVMEIHSKYWRCLQRHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
| OTF | (1S,2S,3S)-1-fluoranyl-2-[4-(5-fluoranylpyrimidin-2-yl)phenyl]-N-oxidanyl-3-phe… | C20 H15 F2 N3 O2 | 2 |
Water and common crystallization additives (NA) are not listed.
Potent, Selective, and Cns-Penetrant Tetrasubstituted Cyclopropane Class Iia Histone Deacetylase (Hdac) Inhibitors. Luckhurst, C.A., Breccia, P., Stott, A.J. et al. ACS Med Chem Lett (2016) 7:34. DOI 10.1021/ACSMEDCHEMLETT.5B00302 · PubMed
Other PDB entries of the same protein (UniProt P56524 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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