8vmj

H3K4me3 nucleosome bound to PRC2_AJ119-450

Method: ELECTRON MICROSCOPY Dmax: 134.2 Å Quality: GOOD

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain I; UniProt 1–136 Chain O; UniProt 1–136 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (157-MER) × 1 Histone H4 × 2 (P62805) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) DNA (157-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–136; UniProt 1–136 Author chain O; PDBConstruct 1–136; UniProt 1–136

Histone H4

Homo sapiens

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain J; UniProt 1–103 Chain Q; UniProt 1–103 Not recorded DNA (157-MER) × 1 Histone H3.2 × 2 (Q71DI3) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) DNA (157-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 3
Chains and sequence ranges Author chain J; PDBConstruct 1–103; UniProt 1–103 Author chain Q; 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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain K; UniProt 13–119 Chain R; UniProt 13–119 Not recorded DNA (157-MER) × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B × 2 (A0A8J1LZU9) DNA (157-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 4
Chains and sequence ranges Author chain K; PDBConstruct 1–107; UniProt 13–119 Author chain R; PDBConstruct 1–107; UniProt 13–119

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain M; UniProt 31–126 Chain S; UniProt 31–126 Not recorded DNA (157-MER) × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A × 2 (Q6AZJ8) DNA (157-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 5
Chains and sequence ranges Author chain M; PDBConstruct 1–96; UniProt 31–126 Author chain S; PDBConstruct 1–96; UniProt 31–126

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 8vmj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vmj
Deposition date deposition_date2024-01-13
Structure title titleH3K4me3 nucleosome bound to PRC2_AJ119-450
Keywords keywordsnucleosome, chromatin, histone, epigenetics, GENE REGULATION, 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_guinier42.24
Radius of gyration Rg (electron density) rg_electron39.40
Forward intensity I(0) i0927015000.00
Molecular weight molecular_weight184050.0 kDa
Excluded volume excluded_volume202880 ų
Envelope volume envelope_volume314440 ų
Hydration-shell volume shell_volume65306 ų
Envelope diameter envelope_diameter141.7
Shell Rg shell_rg46.14
Envelope Rg envelope_rg39.23
Shape Rg shape_rg39.22
Total Rg total_rg40.08
Total atoms total_atoms12540
Residues n_residues1090
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 dmax134.2
Rg (real space) rg_real42.11
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real9.2700e+08
I(0) uncertainty (real space) i0_real_error1.6500e+07
Rg (reciprocal space) rg_reciprocal42.24
I(0) (reciprocal space) i0_reciprocal927100000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.201
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75030000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)