8vmi

PRC2_AJ119-450 bound to H3K4me3

Method: ELECTRON MICROSCOPY Dmax: 150.7 Å Quality: GOOD

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

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–441 Not recorded Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–441; UniProt 1–441

Histone H3.1

Homo sapiens

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 heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 2–7 Non-standard monomer:Yes (specific site not provided by mmCIF) Polycomb protein EED × 1 (O75530) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–6; UniProt 2–7

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain L; UniProt 1–739 Chain T; UniProt 1–739 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 L; PDBConstruct 1–739; UniProt 1–739 Author chain T; PDBConstruct 1–739; UniProt 1–739

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain N; UniProt 1–425 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 N; PDBConstruct 1–425; UniProt 1–425

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–746 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 5
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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain F; UniProt 1–1246 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 F; PDBConstruct 1–1246; UniProt 1–1246

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain P; UniProt 1–301 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Histone H3.1t × 1 (Q16695) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 7
Chains and sequence ranges Author chain P; PDBConstruct 1–301; UniProt 1–301

Histone H3.1t

Homo sapiens

UniProt Q16695

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 26–43 Not recorded Polycomb protein EED × 1 (O75530) Histone H3.1 × 1 (P68431) Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 1 (Q09028) EZH2 × 1 (Q15910) Protein Jumonji × 1 (Q92833) Isoform 3 of Zinc finger protein AEBP2 × 1 (Q6ZN18) ZN ZINC ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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

View Construct and Data Evidence
UniProt name H31T_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–18; UniProt 26–43

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 8vmi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vmi
Deposition date deposition_date2024-01-13
Structure title titlePRC2_AJ119-450 bound to H3K4me3
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_guinier43.74
Radius of gyration Rg (electron density) rg_electron43.61
Forward intensity I(0) i0689850000.00
Molecular weight molecular_weight212430.0 kDa
Excluded volume excluded_volume263990 ų
Envelope volume envelope_volume364040 ų
Hydration-shell volume shell_volume69209 ų
Envelope diameter envelope_diameter165.3
Shell Rg shell_rg48.17
Envelope Rg envelope_rg44.30
Shape Rg shape_rg43.62
Total Rg total_rg43.78
Total atoms total_atoms14940
Residues n_residues1943
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 dmax150.7
Rg (real space) rg_real43.82
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real6.8980e+08
I(0) uncertainty (real space) i0_real_error1.2100e+07
Rg (reciprocal space) rg_reciprocal43.74
I(0) (reciprocal space) i0_reciprocal689800000.0000
Solution quality estimate total_estimate0.8642
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.4
Skewness Skewness skewness0.420
Kurtosis Kurtosis kurtosis-0.156
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha112600000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)