9v9p

Cryo-EM structure of the cPRC1-di-nucleosome (CBX7) complex

Method: ELECTRON MICROSCOPY Dmax: 196.4 Å Quality: GOOD

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

Histone H3.1

OrganismNot specified

UniProt P68431

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Chain K; UniProt 1–136 Chain M; UniProt 1–136 Not recorded Histone H4 × 4 (P62805) Histone H2A type 1-H × 4 (Q96KK5) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
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 Author chain K; PDBConstruct 1–136; UniProt 1–136 Author chain M; PDBConstruct 1–136; UniProt 1–136

Histone H4

OrganismNot specified

UniProt P62805

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Chain Q; UniProt 1–103 Chain R; UniProt 1–103 Not recorded Histone H3.1 × 4 (P68431) Histone H2A type 1-H × 4 (Q96KK5) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
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 Author chain Q; PDBConstruct 1–103; UniProt 1–103 Author chain R; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1-H

OrganismNot specified

UniProt Q96KK5

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain C; UniProt 1–128 Chain G; UniProt 1–128 Chain L; UniProt 1–128 Chain O; UniProt 1–128 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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 H2A1H_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–128; UniProt 1–128 Author chain G; PDBConstruct 1–128; UniProt 1–128 Author chain L; PDBConstruct 1–128; UniProt 1–128 Author chain O; PDBConstruct 1–128; UniProt 1–128

Histone H2B type 1-C/E/F/G/I

OrganismNot specified

UniProt P62807

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Chain N; UniProt 1–126 Chain P; UniProt 1–126 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2A type 1-H × 4 (Q96KK5) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
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 Author chain N; PDBConstruct 1–126; UniProt 1–126 Author chain P; PDBConstruct 1–126; UniProt 1–126

Chromobox protein homolog 7

Homo sapiens

UniProt O95931

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain S; UniProt 1–251 Chain Y; UniProt 1–251 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2A type 1-H × 4 (Q96KK5) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Polycomb complex protein BMI-1 × 2 (P35226) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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.

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

View Construct and Data Evidence
UniProt name CBX7_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–251; UniProt 1–251 Author chain Y; PDBConstruct 1–251; UniProt 1–251

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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain T; UniProt 1–326 Chain V; UniProt 1–326 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2A type 1-H × 4 (Q96KK5) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) E3 ubiquitin-protein ligase RING2 × 2 (Q99496) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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 8
Chains and sequence ranges Author chain T; PDBConstruct 1–326; UniProt 1–326 Author chain V; 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 × 22 DNA 2 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain U; UniProt 1–336 Chain W; UniProt 1–336 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2A type 1-H × 4 (Q96KK5) Histone H2B type 1-C/E/F/G/I × 4 (P62807) DNA (252-MER) × 1 DNA (252-MER) × 1 Chromobox protein homolog 7 × 2 (O95931) Polycomb complex protein BMI-1 × 2 (P35226) ZINC ION × 8 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.40 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 9
Chains and sequence ranges Author chain U; PDBConstruct 1–336; UniProt 1–336 Author chain W; 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 9v9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v9p
Deposition date deposition_date2025-06-01
Structure title titleCryo-EM structure of the cPRC1-di-nucleosome (CBX7) complex
Keywords keywordsnucleosome modification, transcriptional regulation, 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_guinier54.60
Radius of gyration Rg (electron density) rg_electron53.83
Forward intensity I(0) i03196230000.00
Molecular weight molecular_weight367470.0 kDa
Excluded volume excluded_volume416320 ų
Envelope volume envelope_volume714340 ų
Hydration-shell volume shell_volume109170 ų
Envelope diameter envelope_diameter198.9
Shell Rg shell_rg59.17
Envelope Rg envelope_rg52.23
Shape Rg shape_rg53.74
Total Rg total_rg54.18
Total atoms total_atoms46240
Residues n_residues2366
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 dmax196.4
Rg (real space) rg_real54.47
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real3.1960e+09
I(0) uncertainty (real space) i0_real_error6.7570e+07
Rg (reciprocal space) rg_reciprocal54.70
I(0) (reciprocal space) i0_reciprocal3197000000.0000
Solution quality estimate total_estimate0.8480
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.7
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.230
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha306200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.689; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)