8vnz

PRC2_AJ1-450 bound to H3K36me3-modified nucleosome with histone H3 tail disengaged

Method: ELECTRON MICROSCOPY Dmax: 153.5 Å Quality: GOOD

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

Polycomb protein SUZ12

Homo sapiens

UniProt Q15022

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–739 Not recorded Polycomb protein EED × 1 (O75530) Histone-binding protein RBBP4 × 1 (Q09028) Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

29 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUZ12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–739; UniProt 1–739

Polycomb protein EED

Homo sapiens

UniProt O75530

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 1–441 Not recorded Polycomb protein SUZ12 × 1 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

77 other PDB entries and 112 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EED_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–441; UniProt 1–441

Histone-binding protein RBBP4

Homo sapiens

UniProt Q09028

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain N; UniProt 1–425 Not recorded Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

49 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–425; UniProt 1–425

Histone-lysine N-methyltransferase EZH2

Homo sapiens

UniProt Q15910

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–746 Not recorded Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) Histone-binding protein RBBP4 × 1 (Q09028) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

35 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EZH2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–746; UniProt 1–746

Protein Jumonji

Homo sapiens

UniProt Q92833

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 2–450 Non-standard monomer:Yes (specific site not provided by mmCIF) Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) Histone-binding protein RBBP4 × 1 (Q09028) Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name JARD2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 1–449; UniProt 2–450

Isoform 3 of Zinc finger protein AEBP2

Homo sapiens

UniProt Q6ZN18

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain P; UniProt 1–301 Not recorded Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) Histone-binding protein RBBP4 × 1 (Q09028) Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

17 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AEBP2_HUMAN
Isoform Q6ZN18-3
PDB entities 6
Chains and sequence ranges Author chain P; PDBConstruct 1–301; UniProt 1–301

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 8vnz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vnz
Deposition date deposition_date2024-01-14
Structure title titlePRC2_AJ1-450 bound to H3K36me3-modified nucleosome with histone H3 tail disengaged
Keywords keywordscomplex, methyltransferase, histone, epigenetics, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.08
Radius of gyration Rg (electron density) rg_electron42.76
Forward intensity I(0) i0676438000.00
Molecular weight molecular_weight209540.0 kDa
Excluded volume excluded_volume260020 ų
Envelope volume envelope_volume359650 ų
Hydration-shell volume shell_volume69124 ų
Envelope diameter envelope_diameter163.5
Shell Rg shell_rg48.14
Envelope Rg envelope_rg43.37
Shape Rg shape_rg42.78
Total Rg total_rg42.91
Total atoms total_atoms14771
Residues n_residues1960
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 dmax153.5
Rg (real space) rg_real43.14
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real6.7640e+08
I(0) uncertainty (real space) i0_real_error1.2500e+07
Rg (reciprocal space) rg_reciprocal43.08
I(0) (reciprocal space) i0_reciprocal676400000.0000
Solution quality estimate total_estimate0.8647
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.8
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.203
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha143700000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)