9v9x

Cryo-EM structure of the ncPRC1.4 complex containing one RNF2-BMI1 bound to the H2AK119ub-modified nucleosome

Method: ELECTRON MICROSCOPY Dmax: 117.0 Å Quality: GOOD

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

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0TWI5) DNA (130-MER) × 1 DNA (131-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

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 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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0TWI5) DNA (130-MER) × 1 DNA (131-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

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

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Mutation:K119C Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B × 2 (A0A8J0TWI5) DNA (130-MER) × 1 DNA (131-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

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 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

Xenopus laevis

UniProt A0A8J0TWI5

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (130-MER) × 1 DNA (131-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) E3 ubiquitin-protein ligase RING2 × 1 (Q99496) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0TWI5_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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain M; UniProt 1–326 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0TWI5) DNA (130-MER) × 1 DNA (131-MER) × 1 E3 ubiquitin-protein ligase RING2 × 1 (Q99496) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

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 M; 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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain N; UniProt 1–336 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0TWI5) DNA (130-MER) × 1 DNA (131-MER) × 1 Polycomb complex protein BMI-1 × 1 (P35226) ZINC ION × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions 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.

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 N; PDBConstruct 1–336; UniProt 1–336

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 9v9x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v9x
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9v9x
Deposition date deposition_date2025-06-02
Structure title titleCryo-EM structure of the ncPRC1.4 complex containing one RNF2-BMI1 bound to the H2AK119ub-modified nucleosome
Keywords keywordsnucleosome modification, transcriptional regulation, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.28
Radius of gyration Rg (electron density) rg_electron38.98
Forward intensity I(0) i0890732000.00
Molecular weight molecular_weight189530.0 kDa
Excluded volume excluded_volume214380 ų
Envelope volume envelope_volume330080 ų
Hydration-shell volume shell_volume68898 ų
Envelope diameter envelope_diameter119.1
Shell Rg shell_rg46.36
Envelope Rg envelope_rg38.16
Shape Rg shape_rg38.85
Total Rg total_rg39.61
Total atoms total_atoms12967
Residues n_residues1219
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 dmax117.0
Rg (real space) rg_real41.01
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real8.9070e+08
I(0) uncertainty (real space) i0_real_error1.3910e+07
Rg (reciprocal space) rg_reciprocal41.28
I(0) (reciprocal space) i0_reciprocal891000000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.4
Skewness Skewness skewness-0.007
Kurtosis Kurtosis kurtosis-0.655
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49110000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.988; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.516

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)