9dde

ncPRC1RYBP bound to H2AK119Ub/H1.4 chromatosome

Method: ELECTRON MICROSCOPY Dmax: 139.2 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Mutation:G103A Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
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 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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Mutation:G100R, K119C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 3
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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Mutation:S33T Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

Polycomb complex protein BMI-1

Homo sapiens

UniProt P35226

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain K; UniProt 1–326 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMI1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–326; UniProt 1–326

E3 ubiquitin-protein ligase RING2

Homo sapiens

UniProt Q99496

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain L; UniProt 1–336 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

24 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RING2_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–336; UniProt 1–336

RING1 and YY1-binding protein

Homo sapiens

UniProt Q8N488

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain M; UniProt 1–228 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) Ubiquitin × 1 (P0CG47) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

10 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RYBP_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–228; UniProt 1–228

Ubiquitin

Homo sapiens

UniProt P0CG47

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain N; UniProt 1–76 Mutation:G76C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Histone H1.4 × 1 (P10412) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain N; PDBConstruct 1–76; UniProt 1–76

Histone H1.4

Homo sapiens

UniProt P10412

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain O; UniProt 1–219 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (187-MER) × 1 DNA (187-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) RING1 and YY1-binding protein × 1 (Q8N488) Ubiquitin × 1 (P0CG47) ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H14_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain O; PDBConstruct 1–219; UniProt 1–219

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 9dde

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dde
Deposition date deposition_date2024-08-28
Structure title titlencPRC1RYBP bound to H2AK119Ub/H1.4 chromatosome
Keywords keywordsDNA complex protein, 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_guinier44.19
Radius of gyration Rg (electron density) rg_electron41.96
Forward intensity I(0) i01273560000.00
Molecular weight molecular_weight225180.0 kDa
Excluded volume excluded_volume253090 ų
Envelope volume envelope_volume410440 ų
Hydration-shell volume shell_volume79105 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg49.34
Envelope Rg envelope_rg41.16
Shape Rg shape_rg41.85
Total Rg total_rg42.49
Total atoms total_atoms15394
Residues n_residues1471
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 dmax139.2
Rg (real space) rg_real43.90
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.2740e+09
I(0) uncertainty (real space) i0_real_error2.0910e+07
Rg (reciprocal space) rg_reciprocal44.19
I(0) (reciprocal space) i0_reciprocal1274000000.0000
Solution quality estimate total_estimate0.8201
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha90310000.0000
Real-space data points n_real_points37
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: 0.966; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)