8w9e

Cryo-EM structure of the Rpd3S-nucleosome complex from budding yeast in State 2

Method: ELECTRON MICROSCOPY Dmax: 176.8 Å Quality: GOOD

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

Transcriptional regulatory protein SIN3

OrganismNot specified

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain A; UniProt 1–1536 Not recorded Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1536; UniProt 1–1536

Transcriptional regulatory protein RCO1

OrganismNot specified

UniProt Q04779

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain E; UniProt 1–684 Chain F; UniProt 1–684 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RCO1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–684; UniProt 1–684 Author chain F; PDBConstruct 1–684; UniProt 1–684

Histone deacetylase RPD3

OrganismNot specified

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain B; UniProt 1–433 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–433; UniProt 1–433

Chromatin modification-related protein EAF3

OrganismNot specified

UniProt Q12432

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain C; UniProt 1–401 Chain D; UniProt 1–401 Chain G; UniProt 1–401 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

22 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EAF3_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–401; UniProt 1–401 Author chain D; PDBConstruct 1–401; UniProt 1–401 Author chain G; PDBConstruct 1–401; UniProt 1–401

Histone H3.1

OrganismNot specified

UniProt P68431

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain a; UniProt 1–136 Chain e; UniProt 1–136 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain a; PDBConstruct 1–136; UniProt 1–136 Author chain e; PDBConstruct 1–136; UniProt 1–136

Histone H4

OrganismNot specified

UniProt P62805

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain b; UniProt 1–103 Chain f; UniProt 1–103 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain b; PDBConstruct 1–103; UniProt 1–103 Author chain f; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1-B/E

OrganismNot specified

UniProt P04908

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain c; UniProt 1–130 Chain g; UniProt 1–130 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-K × 2 (O60814) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain c; PDBConstruct 1–130; UniProt 1–130 Author chain g; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-K

OrganismNot specified

UniProt O60814

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 × 15 DNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain d; UniProt 1–126 Chain h; UniProt 1–126 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 3 (Q12432) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) 5-DNA × 1 3-DNA × 1 ZN ZINC ION × 7 K POTASSIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain d; PDBConstruct 1–126; UniProt 1–126 Author chain h; PDBConstruct 1–126; UniProt 1–126

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 8w9e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w9e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w9e
Deposition date deposition_date2023-09-05
Structure title titleCryo-EM structure of the Rpd3S-nucleosome complex from budding yeast in State 2
Keywords keywordsRpd3S, HDAC, Sin3, Rpd3, DNA BINDING PROTEIN-DNA COMPLEX; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.92
Radius of gyration Rg (electron density) rg_electron53.15
Forward intensity I(0) i03001310000.00
Molecular weight molecular_weight401920.0 kDa
Excluded volume excluded_volume479220 ų
Envelope volume envelope_volume768310 ų
Hydration-shell volume shell_volume117740 ų
Envelope diameter envelope_diameter179.3
Shell Rg shell_rg59.57
Envelope Rg envelope_rg51.26
Shape Rg shape_rg53.11
Total Rg total_rg53.44
Total atoms total_atoms27886
Residues n_residues2991
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 dmax176.8
Rg (real space) rg_real53.67
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real3.0010e+09
I(0) uncertainty (real space) i0_real_error5.5290e+07
Rg (reciprocal space) rg_reciprocal54.11
I(0) (reciprocal space) i0_reciprocal3003000000.0000
Solution quality estimate total_estimate0.8776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.2
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha317800000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)