8kd7

Rpd3S in complex with nucleosome with H3K36MLA modification and 167bp DNA

Method: ELECTRON MICROSCOPY Dmax: 148.2 Å Quality: GOOD

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

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 Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 1
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 Histone deacetylase RPD3 × 1 (P32561) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 2
Chains and sequence ranges Author chain B; PDBConstruct 50–1371; UniProt 215–1536

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 deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 F; 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain E; UniProt 1–684 Chain G; UniProt 1–684 Not recorded Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) 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) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 E; 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 × 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) Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 5
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 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 6
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 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 7
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 Histone deacetylase RPD3 × 1 (P32561) Transcriptional regulatory protein SIN3 × 1 (P22579) Chromatin modification-related protein EAF3 × 2 (Q12432) Transcriptional regulatory protein RCO1 × 2 (Q04779) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) 167bp DNA × 1 167bp DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 8
Chains and sequence ranges Author chain R; PDBConstruct 1–122; UniProt 5–126 Author chain V; PDBConstruct 1–122; 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 8kd7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8kd7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8kd7
Deposition date deposition_date2023-08-09
Structure title titleRpd3S in complex with nucleosome with H3K36MLA modification and 167bp DNA
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_guinier49.39
Radius of gyration Rg (electron density) rg_electron48.08
Forward intensity I(0) i02537840000.00
Molecular weight molecular_weight359270.0 kDa
Excluded volume excluded_volume424260 ų
Envelope volume envelope_volume658950 ų
Hydration-shell volume shell_volume109230 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg56.45
Envelope Rg envelope_rg46.70
Shape Rg shape_rg48.00
Total Rg total_rg48.53
Total atoms total_atoms24894
Residues n_residues2602
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 dmax148.2
Rg (real space) rg_real48.96
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real2.5380e+09
I(0) uncertainty (real space) i0_real_error3.5240e+07
Rg (reciprocal space) rg_reciprocal49.39
I(0) (reciprocal space) i0_reciprocal2539000000.0000
Solution quality estimate total_estimate0.8726
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.5
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha400700000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.593

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8kd7A01
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)