7ksr

PRC2:EZH1_A from a dimeric PRC2 bound to a nucleosome

Method: ELECTRON MICROSCOPY Dmax: 153.1 Å Quality: GOOD

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

Histone-lysine N-methyltransferase EZH1

Homo sapiens

UniProt Q92800

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–747 Not recorded Histone-binding protein RBBP4 × 1 (Q09028) Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EZH1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–747; UniProt 1–747

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–425 Not recorded Histone-lysine N-methyltransferase EZH1 × 1 (Q92800) Polycomb protein SUZ12 × 1 (Q15022) Polycomb protein EED × 1 (O75530) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–425; UniProt 1–425

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–739 Not recorded Histone-lysine N-methyltransferase EZH1 × 1 (Q92800) Histone-binding protein RBBP4 × 1 (Q09028) Polycomb protein EED × 1 (O75530) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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 C; 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–441 Not recorded Histone-lysine N-methyltransferase EZH1 × 1 (Q92800) Histone-binding protein RBBP4 × 1 (Q09028) Polycomb protein SUZ12 × 1 (Q15022) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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 4
Chains and sequence ranges Author chain B; 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 7ksr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ksr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7ksr
Deposition date deposition_date2020-11-24
Structure title titlePRC2:EZH1_A from a dimeric PRC2 bound to a nucleosome
Keywords keywordsChromatin, methyltransferase, nucleosome-modifying complex, GENE REGULATION, GENE REGULATION-Transferase complex; GENE REGULATION/Transferase
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.05
Radius of gyration Rg (electron density) rg_electron49.13
Forward intensity I(0) i0440259000.00
Molecular weight molecular_weight168970.0 kDa
Excluded volume excluded_volume209340 ų
Envelope volume envelope_volume328170 ų
Hydration-shell volume shell_volume56425 ų
Envelope diameter envelope_diameter163.6
Shell Rg shell_rg50.99
Envelope Rg envelope_rg49.54
Shape Rg shape_rg49.17
Total Rg total_rg49.08
Total atoms total_atoms11863
Residues n_residues1524
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 dmax153.1
Rg (real space) rg_real49.33
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real4.4030e+08
I(0) uncertainty (real space) i0_real_error9.1260e+06
Rg (reciprocal space) rg_reciprocal49.06
I(0) (reciprocal space) i0_reciprocal440100000.0000
Solution quality estimate total_estimate0.8239
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary67.0
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.581
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38300000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.022

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)