Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor. Determined by X-ray diffraction at 2.15 Å resolution. Released 5 Dec 2018.
Explore 6FYZ in 3D Show helices and sheets RCSB PDB PDBe
6FYZ contains 65 α-helices and 44 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 |
|---|---|---|---|
| β-strand | 654-657 | 4 | 1 |
| α-helix | 660-664 | 5 | |
| α-helix | 680-691 | 12 | |
| α-helix | 695-697 | 3 | |
| β-strand | 699-701 | 3 | 1 |
| α-helix | 705-707 | 3 | |
| α-helix | 708-711 | 4 | |
| α-helix | 717-724 | 8 | |
| α-helix | 767-786 | 20 | |
| β-strand | 792-795 | 4 | 1 |
| β-strand | 810 | 1 | 2 |
| β-strand | 813 | 1 | 2 |
| α-helix | 817-828 | 12 | |
| 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 | 901-902 | 2 | |
| β-strand | 903 | 1 | 3 |
| 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 | 947 | 1 | 3 |
| β-strand | 948 | 1 | 4 |
| α-helix | 950-961 | 12 | |
| α-helix | 964-966 | 3 | |
| β-strand | 968-972 | 5 | 1 |
| α-helix | 978-992 | 15 | |
| α-helix | 1007-1010 | 4 | |
| α-helix | 1011-1024 | 14 | |
| α-helix | 1029-1031 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 654-657 | 4 | 5 |
| α-helix | 660-664 | 5 | |
| α-helix | 680-691 | 12 | |
| β-strand | 699-701 | 3 | 5 |
| α-helix | 705-707 | 3 | |
| α-helix | 708-711 | 4 | |
| α-helix | 717-724 | 8 | |
| β-strand | 755-757 | 3 | 6 |
| β-strand | 760-761 | 2 | 6 |
| α-helix | 767-786 | 20 | |
| β-strand | 792-795 | 4 | 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 | 866-868 | 3 | |
| 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 | 978-993 | 16 | |
| α-helix | 1000-1002 | 3 | |
| α-helix | 1003-1006 | 4 | |
| α-helix | 1008-1011 | 4 | |
| α-helix | 1012-1025 | 14 | |
| α-helix | 1030-1032 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 654-657 | 4 | 9 |
| α-helix | 660-664 | 5 | |
| α-helix | 680-691 | 12 | |
| α-helix | 694-697 | 4 | |
| β-strand | 699-701 | 3 | 9 |
| α-helix | 702 | 1 | |
| α-helix | 705-707 | 3 | |
| α-helix | 708-711 | 4 | |
| α-helix | 717-724 | 8 | |
| α-helix | 767-786 | 20 | |
| β-strand | 792-795 | 4 | 9 |
| β-strand | 805 | 1 | 10 |
| β-strand | 808 | 1 | 10 |
| β-strand | 810 | 1 | 11 |
| β-strand | 813 | 1 | 11 |
| α-helix | 817-829 | 13 | |
| β-strand | 834-838 | 5 | 9 |
| α-helix | 845-851 | 7 | |
| β-strand | 857-864 | 8 | 9 |
| α-helix | 866-868 | 3 | |
| α-helix | 883-885 | 3 | |
| β-strand | 889-894 | 6 | 9 |
| β-strand | 903 | 1 | 12 |
| α-helix | 904-910 | 7 | |
| α-helix | 911-915 | 5 | |
| α-helix | 916-922 | 7 | |
| β-strand | 926-931 | 6 | 9 |
| β-strand | 936 | 1 | 13 |
| β-strand | 947 | 1 | 12 |
| β-strand | 948 | 1 | 13 |
| α-helix | 950-961 | 12 | |
| α-helix | 964-966 | 3 | |
| β-strand | 968-972 | 5 | 9 |
| α-helix | 978-992 | 15 | |
| α-helix | 1004-1006 | 3 | |
| 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, C | protein | 395 | Homo sapiens | P56524 (AlphaFold model) |
>6FYZ_1 Histone deacetylase 4 (chains A, B, C) MGSTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGR KATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNE VHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKL LQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGP GVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLG GYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKV LQQRPNANAVRSMEKVMEIHSKYWRCLQRHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| EBE | (2~{S})-2-(2-fluorophenyl)-2-[4-(2-methylpyrimidin-5-yl)phenyl]-~{N}-oxidanyl-e… | C19 H16 F N3 O2 | 3 |
| ZN | Zinc ion | Zn | 6 |
Water and common crystallization additives (NA) are not listed.
Development and characterization of a CNS-penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor. Luckhurst, C.A., Aziz, O., Beaumont, V. et al. Bioorg Med Chem Lett (2019) 29:83-88. DOI 10.1016/j.bmcl.2018.11.009 · 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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