5h14

EED in complex with an allosteric PRC2 inhibitor EED666

Method: X-RAY DIFFRACTION Dmax: 104.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 76–441 Fragment:UNP residues 76-441 Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) GOL GLYCEROL × 1 LQB 2-[3-(3,5-dimethylpyrazol-1-yl)-4-nitro-phenyl]-3,4-dihydro-1H-isoquinoline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M Tris, 16% PEG 8000, 10 mM beta-Nicotinamide mononucleotide Resolution 1.90 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 76–441 Fragment:UNP residues 76-441 Histone-lysine N-methyltransferase EZH2 × 1 (Q15910) GOL GLYCEROL × 1 LQB 2-[3-(3,5-dimethylpyrazol-1-yl)-4-nitro-phenyl]-3,4-dihydro-1H-isoquinoline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M Tris, 16% PEG 8000, 10 mM beta-Nicotinamide mononucleotide Resolution 1.90 Å R-free 0.223

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 111 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 2–367; UniProt 76–441 Author chain B; PDBConstruct 2–367; UniProt 76–441

Histone-lysine N-methyltransferase EZH2

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 40–68 Fragment:UNP residues 40-68 Polycomb protein EED × 1 (O75530) GOL GLYCEROL × 1 LQB 2-[3-(3,5-dimethylpyrazol-1-yl)-4-nitro-phenyl]-3,4-dihydro-1H-isoquinoline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M Tris, 16% PEG 8000, 10 mM beta-Nicotinamide mononucleotide Resolution 1.90 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 40–68 Fragment:UNP residues 40-68 Polycomb protein EED × 1 (O75530) GOL GLYCEROL × 1 LQB 2-[3-(3,5-dimethylpyrazol-1-yl)-4-nitro-phenyl]-3,4-dihydro-1H-isoquinoline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1 M Tris, 16% PEG 8000, 10 mM beta-Nicotinamide mononucleotide Resolution 1.90 Å R-free 0.223

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 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EZH2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–29; UniProt 40–68 Author chain D; PDBConstruct 1–29; UniProt 40–68

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 5h14

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h14
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h14
Deposition date deposition_date2016-10-08
Structure title titleEED in complex with an allosteric PRC2 inhibitor EED666
Keywords keywordsEED, PRC2, inhibitor, Transferase-Transferase Inhibitor complex; Transferase/Transferase Inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.80
Radius of gyration Rg (electron density) rg_electron32.11
Forward intensity I(0) i0133875000.00
Molecular weight molecular_weight91293.0 kDa
Excluded volume excluded_volume113730 ų
Envelope volume envelope_volume141750 ų
Hydration-shell volume shell_volume37122 ų
Envelope diameter envelope_diameter107.2
Shell Rg shell_rg39.00
Envelope Rg envelope_rg31.43
Shape Rg shape_rg32.08
Total Rg total_rg32.74
Total atoms total_atoms6419
Residues n_residues780
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 dmax104.2
Rg (real space) rg_real32.89
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.3390e+08
I(0) uncertainty (real space) i0_real_error2.2390e+06
Rg (reciprocal space) rg_reciprocal32.86
I(0) (reciprocal space) i0_reciprocal133900000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.761
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha68720000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5h14A00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id5h14B00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)