8w9c

Cryo-EM structure of the Rpd3S complex from budding yeast

Method: ELECTRON MICROSCOPY Dmax: 162.3 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1536 Not recorded Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) ZN ZINC ION × 7 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count 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 × 2 (Q12432) ZN ZINC ION × 7 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–433 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Chromatin modification-related protein EAF3 × 2 (Q12432) ZN ZINC ION × 7 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–401 Chain D; UniProt 1–401 Not recorded Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone deacetylase RPD3 × 1 (P32561) ZN ZINC ION × 7 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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

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 8w9c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w9c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w9c
Deposition date deposition_date2023-09-05
Structure title titleCryo-EM structure of the Rpd3S complex from budding yeast
Keywords keywordsRpd3S, HDAC, Sin3, Rpd3, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.26
Radius of gyration Rg (electron density) rg_electron47.05
Forward intensity I(0) i0670559000.00
Molecular weight molecular_weight217390.0 kDa
Excluded volume excluded_volume273160 ų
Envelope volume envelope_volume386580 ų
Hydration-shell volume shell_volume69620 ų
Envelope diameter envelope_diameter166.0
Shell Rg shell_rg49.76
Envelope Rg envelope_rg46.99
Shape Rg shape_rg47.02
Total Rg total_rg47.26
Total atoms total_atoms15278
Residues n_residues1868
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 dmax162.3
Rg (real space) rg_real47.37
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real6.7060e+08
I(0) uncertainty (real space) i0_real_error1.3540e+07
Rg (reciprocal space) rg_reciprocal47.27
I(0) (reciprocal space) i0_reciprocal670500000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.1
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76160000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.879

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)