8tof

Rpd3S bound to an H3K36Cme3 modified nucleosome

Method: ELECTRON MICROSCOPY Dmax: 178.2 Å Quality: GOOD

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

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain A; UniProt 1–1536 Not recorded Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain B; UniProt 1–433 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–433; UniProt 1–433

Chromatin modification-related protein EAF3

Saccharomyces cerevisiae

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain D; UniProt 1–401 Chain E; UniProt 1–401 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–401; UniProt 1–401 Author chain E; PDBConstruct 1–401; UniProt 1–401

Transcriptional regulatory protein RCO1

Saccharomyces cerevisiae

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain F; UniProt 1–684 Chain G; UniProt 1–684 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 4
Chains and sequence ranges Author chain F; PDBConstruct 1–684; UniProt 1–684 Author chain G; PDBConstruct 1–684; UniProt 1–684

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain a; UniProt 1–136 Chain e; UniProt 1–136 Non-standard monomer:Yes (specific site not provided by mmCIF) Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 8
Chains and sequence ranges Author chain a; PDBConstruct 1–136; UniProt 1–136 Author chain e; PDBConstruct 1–136; UniProt 1–136

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain b; UniProt 14–116 Chain f; UniProt 14–116 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 9
Chains and sequence ranges Author chain b; PDBConstruct 1–103; UniProt 14–116 Author chain f; PDBConstruct 1–103; UniProt 14–116

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain c; UniProt 1–130 Chain g; UniProt 1–130 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2B 1.1 × 2 (P02281) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 10
Chains and sequence ranges Author chain c; PDBConstruct 1–130; UniProt 1–130 Author chain g; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain d; UniProt 5–126 Chain h; UniProt 5–126 Mutation:S29T Transcriptional regulatory protein SIN3 × 1 (P22579) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Rco1 × 1 DNA (176-MER) × 1 DNA (176-MER) × 1 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) histone N-terminal tail × 1 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 11
Chains and sequence ranges Author chain d; PDBConstruct 2–123; UniProt 5–126 Author chain h; PDBConstruct 2–123; UniProt 5–126

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 8tof

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tof
Deposition date deposition_date2023-08-03
Structure title titleRpd3S bound to an H3K36Cme3 modified nucleosome
Keywords keywordsnucleosome, methylation, acetylation, Rpd3S, TRANSCRIPTION, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.73
Radius of gyration Rg (electron density) rg_electron55.23
Forward intensity I(0) i03421580000.00
Molecular weight molecular_weight420290.0 kDa
Excluded volume excluded_volume496570 ų
Envelope volume envelope_volume786380 ų
Hydration-shell volume shell_volume116680 ų
Envelope diameter envelope_diameter189.1
Shell Rg shell_rg60.41
Envelope Rg envelope_rg53.74
Shape Rg shape_rg55.19
Total Rg total_rg55.47
Total atoms total_atoms29102
Residues n_residues3049
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 dmax178.2
Rg (real space) rg_real55.55
Rg uncertainty (real space) rg_real_error1.87
I(0) (real space) i0_real3.4220e+09
I(0) uncertainty (real space) i0_real_error6.5910e+07
Rg (reciprocal space) rg_reciprocal55.87
I(0) (reciprocal space) i0_reciprocal3423000000.0000
Solution quality estimate total_estimate0.8716
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary171.8
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.299
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha248700000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.665

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)