8hy0

Composite cryo-EM structure of the histone deacetylase complex Rpd3S in complex with nucleosome

Method: ELECTRON MICROSCOPY Dmax: 195.9 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Mutation:C110A Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt A0A8J1LTD2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain B; UniProt 15–116 Chain F; UniProt 15–116 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J1LTD2_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 15–116 Author chain F; PDBConstruct 1–102; UniProt 15–116

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B

Xenopus laevis

UniProt A0A8J0U496

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0U496_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

Transcriptional regulatory protein SIN3

Saccharomyces cerevisiae

UniProt P22579

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain K; UniProt 1–1536 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIN3_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–1536; UniProt 1–1536

Histone deacetylase RPD3

Saccharomyces cerevisiae

UniProt P32561

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain L; UniProt 1–433 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPD3_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–433; UniProt 1–433

Chromatin modification-related protein EAF3

Saccharomyces cerevisiae

UniProt A0A8H4F719

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain M; UniProt 1–401 Chain O; UniProt 1–401 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) RCO1 isoform 1 × 2 (A0A8H4BXB0) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4F719_YEASX
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–401; UniProt 1–401 Author chain O; PDBConstruct 1–401; UniProt 1–401

RCO1 isoform 1

Saccharomyces cerevisiae

UniProt A0A8H4BXB0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain N; UniProt 1–684 Chain P; UniProt 1–684 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (352-MER) × 1 DNA (352-MER) × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (A0A8H4F719) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-Na pH 7.5, 40 mM KCl, 2 mM MgCl2, 1 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4BXB0_YEASX
Isoform
PDB entities 10
Chains and sequence ranges Author chain N; PDBConstruct 1–684; UniProt 1–684 Author chain P; PDBConstruct 1–684; UniProt 1–684

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8hy0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8hy0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8hy0
Deposition date deposition_date2023-01-05
Structure title titleComposite cryo-EM structure of the histone deacetylase complex Rpd3S in complex with nucleosome
Keywords keywordsHistone deacetylase complex, nucleosome, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier56.92
Radius of gyration Rg (electron density) rg_electron56.75
Forward intensity I(0) i03322050000.00
Molecular weight molecular_weight416140.0 kDa
Excluded volume excluded_volume492590 ų
Envelope volume envelope_volume787250 ų
Hydration-shell volume shell_volume114720 ų
Envelope diameter envelope_diameter191.1
Shell Rg shell_rg60.77
Envelope Rg envelope_rg55.26
Shape Rg shape_rg56.71
Total Rg total_rg56.95
Total atoms total_atoms28821
Residues n_residues3030
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax195.9
Rg (real space) rg_real59.02
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real3.3160e+09
I(0) uncertainty (real space) i0_real_error6.2900e+07
Rg (reciprocal space) rg_reciprocal56.99
I(0) (reciprocal space) i0_reciprocal3323000000.0000
Solution quality estimate total_estimate0.6754
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.0
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis0.019
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha1.1700
Highest regularization parameter α highest_alpha257300000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 0.891; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.603

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)