4BKX: HDAC1

The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 3 Jul 2013.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
4,262
Mol. weight
75.73 kDa
Ligands
ZN
Released
3 Jul 2013

Explore 4BKX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BKX contains 27 α-helices and 17 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.

Chain A: 9 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix175-1828
β-strand195-19951
α-helix207-22418
α-helix238-2469
α-helix248-26013
α-helix265-2728
α-helix284-2874
α-helix290-30314
α-helix307-3137
α-helix320-33011
Chain B: 18 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand11-1441
α-helix19-213
α-helix33-4412
α-helix48-503
β-strand52-5651
α-helix57-604
α-helix61-644
α-helix70-789
α-helix88-947
β-strand9612
β-strand10012
α-helix106-12520
β-strand131-13441
β-strand14813
β-strand15113
α-helix155-1639
β-strand170-17451
α-helix181-1866
β-strand193-20081
α-helix217-2193
β-strand223-22861
α-helix234-25219
β-strand256-26051
α-helix263-2653
β-strand26614
β-strand27614
α-helix278-28912
β-strand295-29841
α-helix305-31915
β-strand32715
α-helix328-3303
α-helix334-3363
β-strand34215
α-helix356-37116

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Metastasis-associated protein MTA1Aprotein176HOMO SAPIENSQ13330 (AlphaFold model)
Histone deacetylase 1Bprotein482HOMO SAPIENSQ13547 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4BKX_1 METASTASIS-ASSOCIATED PROTEIN MTA1 (chains A)
GAADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARS
VGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPV
LCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDR
Sequence of entity 2 (B), FASTA
>4BKX_2 HISTONE DEACETYLASE 1 (chains B)
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKAN
AEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAS
AVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHG
DGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAI
FKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGG
GGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLE
KIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEF
SDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVK
LA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Water and common crystallization additives (ACT, K, SO4) are not listed.

Primary citation

Class I Hdacs Share a Common Mechanism of Regulation by Inositol Phosphates. Millard, C.J., Watson, P.J., Celardo, I. et al. Mol Cell (2013) 51:57. DOI 10.1016/J.MOLCEL.2013.05.020 · PubMed

Other PDB entries of the same protein (UniProt Q13330 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 4BKX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.