8kd6

Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class3

Method: ELECTRON MICROSCOPY Dmax: 164.3 Å Quality: GOOD

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

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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain D; UniProt 1–401 Chain F; UniProt 1–401 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 1
Chains and sequence ranges Author chain D; PDBConstruct 1–401; UniProt 1–401 Author chain F; PDBConstruct 1–401; UniProt 1–401

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 O; UniProt 2–136 Chain S; UniProt 2–136 Mutation:C110A Non-standard monomer:Yes (specific site not provided by mmCIF) Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 2
Chains and sequence ranges Author chain O; PDBConstruct 1–135; UniProt 2–136 Author chain S; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

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 P; UniProt 2–103 Chain T; UniProt 2–103 Not recorded Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–102; UniProt 2–103 Author chain T; PDBConstruct 1–102; UniProt 2–103

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 Q; UniProt 2–130 Chain U; UniProt 2–130 Not recorded Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 4
Chains and sequence ranges Author chain Q; PDBConstruct 1–129; UniProt 2–130 Author chain U; PDBConstruct 1–129; UniProt 2–130

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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain R; UniProt 5–126 Chain V; UniProt 5–126 Mutation:S29T Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 5
Chains and sequence ranges Author chain R; PDBConstruct 1–122; UniProt 5–126 Author chain V; PDBConstruct 1–122; UniProt 5–126

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 A; UniProt 1–433 Not recorded Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 A; PDBConstruct 1–433; UniProt 1–433

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 B; UniProt 215–1536 Not recorded Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein RCO1 × 2 (Q04779) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 9
Chains and sequence ranges Author chain B; PDBConstruct 50–1371; UniProt 215–1536

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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain E; UniProt 1–684 Chain G; UniProt 1–684 Not recorded Chromatin modification-related protein EAF3 × 2 (Q12432) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 187bp DNA × 1 187bp DNA × 1 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 10
Chains and sequence ranges Author chain E; PDBConstruct 1–684; UniProt 1–684 Author chain G; 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 8kd6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8kd6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8kd6
Deposition date deposition_date2023-08-09
Structure title titleRpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class3
Keywords keywordsRpd3S, HDAC, Hho1, cryptic transcription, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.19
Radius of gyration Rg (electron density) rg_electron51.42
Forward intensity I(0) i02955940000.00
Molecular weight molecular_weight389360.0 kDa
Excluded volume excluded_volume460040 ų
Envelope volume envelope_volume726600 ų
Hydration-shell volume shell_volume114150 ų
Envelope diameter envelope_diameter174.8
Shell Rg shell_rg58.24
Envelope Rg envelope_rg50.24
Shape Rg shape_rg51.36
Total Rg total_rg51.76
Total atoms total_atoms26982
Residues n_residues2815
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 dmax164.3
Rg (real space) rg_real51.99
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real2.9560e+09
I(0) uncertainty (real space) i0_real_error4.7970e+07
Rg (reciprocal space) rg_reciprocal52.35
I(0) (reciprocal space) i0_reciprocal2957000000.0000
Solution quality estimate total_estimate0.8750
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.2
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha327000000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.734

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8kd6A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology800 — Arginase; Chain A
Homologous superfamily homologous superfamily20 — Histone deacetylase domain

8. Citations (1)

9. Files and Curves (10)