9dch

Single-stranded RNA-mediated PRC2 dimer

Method: ELECTRON MICROSCOPY Dmax: 233.2 Å Quality: GOOD

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

Isoform 2 of 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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain A; UniProt 2–751 Chain H; UniProt 2–751 Not recorded TERRAmut RNA × 1 Polycomb protein SUZ12 × 2 (Q15022) RBAP48 × 2 (Q09028) Zinc finger protein AEBP2 × 2 (Q6ZN18) Protein Jumonji × 2 (Q92833) Polycomb protein EED × 2 (O75530) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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 Q15910-2
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–750; UniProt 2–751 Author chain H; PDBConstruct 1–750; UniProt 2–751

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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain B; UniProt 1–739 Chain I; UniProt 1–739 Not recorded TERRAmut RNA × 1 Isoform 2 of Histone-lysine N-methyltransferase EZH2 × 2 (Q15910) RBAP48 × 2 (Q09028) Zinc finger protein AEBP2 × 2 (Q6ZN18) Protein Jumonji × 2 (Q92833) Polycomb protein EED × 2 (O75530) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–727; UniProt 1–739 Author chain I; PDBConstruct 1–727; UniProt 1–739

RBAP48

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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain D; UniProt 1–425 Chain K; UniProt 1–425 Not recorded TERRAmut RNA × 1 Isoform 2 of Histone-lysine N-methyltransferase EZH2 × 2 (Q15910) Polycomb protein SUZ12 × 2 (Q15022) Zinc finger protein AEBP2 × 2 (Q6ZN18) Protein Jumonji × 2 (Q92833) Polycomb protein EED × 2 (O75530) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–425; UniProt 1–425 Author chain K; PDBConstruct 1–425; UniProt 1–425

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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain F; UniProt 210–503 Chain M; UniProt 210–503 Not recorded TERRAmut RNA × 1 Isoform 2 of Histone-lysine N-methyltransferase EZH2 × 2 (Q15910) Polycomb protein SUZ12 × 2 (Q15022) RBAP48 × 2 (Q09028) Protein Jumonji × 2 (Q92833) Polycomb protein EED × 2 (O75530) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–294; UniProt 210–503 Author chain M; PDBConstruct 1–294; UniProt 210–503

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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain E; UniProt 119–450 Chain L; UniProt 119–450 Not recorded TERRAmut RNA × 1 Isoform 2 of Histone-lysine N-methyltransferase EZH2 × 2 (Q15910) Polycomb protein SUZ12 × 2 (Q15022) RBAP48 × 2 (Q09028) Zinc finger protein AEBP2 × 2 (Q6ZN18) Polycomb protein EED × 2 (O75530) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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 6
Chains and sequence ranges Author chain E; PDBConstruct 1–332; UniProt 119–450 Author chain L; PDBConstruct 1–332; UniProt 119–450

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–RNA Heteromer Protein × 12 RNA 1 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain C; UniProt 1–441 Chain J; UniProt 1–441 Not recorded TERRAmut RNA × 1 Isoform 2 of Histone-lysine N-methyltransferase EZH2 × 2 (Q15910) Polycomb protein SUZ12 × 2 (Q15022) RBAP48 × 2 (Q09028) Zinc finger protein AEBP2 × 2 (Q6ZN18) Protein Jumonji × 2 (Q92833) ZN ZINC ION × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;RNP complex buffer (25 mM HEPES pH 7.9, 50 mM KCl, 2 mM MgCl2, 10% glycerol, and 1 mM TCEP) EM preparation buffer I (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, and 1 mM TCEP) EM preparation buffer II (25 mM HEPES pH 7.9, 50 mM KCl, 2.5% glycerol, 0.01%NP-40, and 1 mM TCEP). cryo-EM vitrification conditions:Cryogen ETHANE;2-3s of single side blotting 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.

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 7
Chains and sequence ranges Author chain C; PDBConstruct 1–441; UniProt 1–441 Author chain J; PDBConstruct 1–441; UniProt 1–441

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 9dch

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dch
Deposition date deposition_date2024-08-26
Structure title titleSingle-stranded RNA-mediated PRC2 dimer
Keywords keywordsPRC2, RNA, RNP complex, chromatin modifier, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.63
Radius of gyration Rg (electron density) rg_electron66.30
Forward intensity I(0) i01934740000.00
Molecular weight molecular_weight345230.0 kDa
Excluded volume excluded_volume419750 ų
Envelope volume envelope_volume727920 ų
Hydration-shell volume shell_volume94311 ų
Envelope diameter envelope_diameter244.4
Shell Rg shell_rg62.58
Envelope Rg envelope_rg64.77
Shape Rg shape_rg66.46
Total Rg total_rg65.70
Total atoms total_atoms24433
Residues n_residues3596
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 dmax233.2
Rg (real space) rg_real66.22
Rg uncertainty (real space) rg_real_error2.70
I(0) (real space) i0_real1.9350e+09
I(0) uncertainty (real space) i0_real_error4.0030e+07
Rg (reciprocal space) rg_reciprocal65.05
I(0) (reciprocal space) i0_reciprocal1931000000.0000
Solution quality estimate total_estimate0.8408
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.0
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha79360000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.666

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)