9v2v

Cryo-EM structure of the histone deacetylase complex Rpd3L in complex with mono-nucleosome

Method: ELECTRON MICROSCOPY Dmax: 217.0 Å Quality: GOOD

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

Transcriptional regulatory protein SIN3

Saccharomyces cerevisiae S288C

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain A; UniProt 662–1344 Chain B; UniProt 662–1344 Not recorded Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1–683; UniProt 662–1344 Author chain B; PDBConstruct 1–683; UniProt 662–1344

Histone deacetylase RPD3

Saccharomyces cerevisiae S288C

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain C; UniProt 9–393 Chain D; UniProt 9–393 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 C; PDBConstruct 1–385; UniProt 9–393 Author chain D; PDBConstruct 1–385; UniProt 9–393

Transcriptional regulatory protein DEP1

Saccharomyces cerevisiae S288C

UniProt P31385

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain E; UniProt 177–295 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DEP1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–119; UniProt 177–295

Transcriptional regulatory protein SDS3

Saccharomyces cerevisiae S288C

UniProt P40505

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain F; UniProt 14–324 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDS3_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–311; UniProt 14–324

Transcriptional regulatory protein SAP30

Saccharomyces cerevisiae S288C

UniProt P38429

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain G; UniProt 71–191 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAP30_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–121; UniProt 71–191

Transcriptional regulatory protein RXT3

Saccharomyces cerevisiae S288C

UniProt Q07458

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain H; UniProt 64–274 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RXT3_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–211; UniProt 64–274

Transcriptional regulatory protein PHO23

Saccharomyces cerevisiae S288C

UniProt P50947

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain I; UniProt 11–115 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHO23_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain I; PDBConstruct 1–105; UniProt 11–115

Transcriptional regulatory protein RXT2

Saccharomyces cerevisiae S288C

UniProt P38255

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain J; UniProt 157–374 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RXT2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain J; PDBConstruct 1–218; UniProt 157–374

Histone deacetylase complex subunit CTI6

Saccharomyces cerevisiae S288C

UniProt Q08923

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain K; UniProt 243–491 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTI6_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain K; PDBConstruct 1–249; UniProt 243–491

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain O; UniProt 12–118 Chain S; UniProt 12–118 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 O; PDBConstruct 1–107; UniProt 12–118 Author chain S; PDBConstruct 1–107; UniProt 12–118

Histone H2B

Xenopus laevis

UniProt A0A8J1LZU9

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain P; UniProt 32–124 Chain T; UniProt 32–124 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J1LZU9_XENLA
Isoform
PDB entities 11
Chains and sequence ranges Author chain P; PDBConstruct 1–93; UniProt 32–124 Author chain T; PDBConstruct 1–93; UniProt 32–124

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain Q; UniProt 38–135 Chain U; UniProt 38–135 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H4 × 2 (P62799) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 12
Chains and sequence ranges Author chain Q; PDBConstruct 1–98; UniProt 38–135 Author chain U; PDBConstruct 1–98; UniProt 38–135

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain R; UniProt 23–101 Chain V; UniProt 23–101 Not recorded Transcriptional regulatory protein SIN3 × 2 (P22579) Histone deacetylase RPD3 × 2 (P32561) Transcriptional regulatory protein DEP1 × 1 (P31385) Transcriptional regulatory protein SDS3 × 1 (P40505) Transcriptional regulatory protein SAP30 × 1 (P38429) Transcriptional regulatory protein RXT3 × 1 (Q07458) Transcriptional regulatory protein PHO23 × 1 (P50947) Transcriptional regulatory protein RXT2 × 1 (P38255) Histone deacetylase complex subunit CTI6 × 1 (Q08923) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3 × 2 (A0A310TTQ1) DNA (155-MER) × 1 DNA (155-MER) × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 13
Chains and sequence ranges Author chain R; PDBConstruct 1–79; UniProt 23–101 Author chain V; PDBConstruct 1–79; UniProt 23–101

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 9v2v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v2v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v2v
Deposition date deposition_date2025-05-21
Structure title titleCryo-EM structure of the histone deacetylase complex Rpd3L in complex with mono-nucleosome
Keywords keywords;Histone deacetylase complex, Histone modification, Rpd3L, Cryo-EM, mono-nucleosome, GENE REGULATION/DNA, GENE REGULATION-DNA complex ;; GENE REGULATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.27
Radius of gyration Rg (electron density) rg_electron67.11
Forward intensity I(0) i04320480000.00
Molecular weight molecular_weight491830.0 kDa
Excluded volume excluded_volume589520 ų
Envelope volume envelope_volume942530 ų
Hydration-shell volume shell_volume119820 ų
Envelope diameter envelope_diameter238.9
Shell Rg shell_rg64.05
Envelope Rg envelope_rg66.22
Shape Rg shape_rg67.05
Total Rg total_rg67.25
Total atoms total_atoms34241
Residues n_residues3721
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 dmax217.0
Rg (real space) rg_real67.51
Rg uncertainty (real space) rg_real_error2.05
I(0) (real space) i0_real4.3190e+09
I(0) uncertainty (real space) i0_real_error9.1600e+07
Rg (reciprocal space) rg_reciprocal66.21
I(0) (reciprocal space) i0_reciprocal4310000000.0000
Solution quality estimate total_estimate0.8268
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.527
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha198700000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.100

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)