6v3y

Crystal structure of EED in complex with PALI1-K1219me3 peptide

Method: X-RAY DIFFRACTION Dmax: 68.0 Å Quality: REASONABLE

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 81–439 Fragment:UNP residues 81-439 PALI1 peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;3.6 M sodium formate, 10 mM TCEP, 5% glycerol Resolution 1.63 Å R-free 0.193

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 1–359; UniProt 81–439

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 6v3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6v3y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6v3y
Deposition date deposition_date2019-11-26
Structure title titleCrystal structure of EED in complex with PALI1-K1219me3 peptide
Keywords keywordsEED, PALI1, tri-methyl-lysine, LCOR, C10ORF12, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.91
Radius of gyration Rg (electron density) rg_electron19.68
Forward intensity I(0) i029019500.00
Molecular weight molecular_weight41029.0 kDa
Excluded volume excluded_volume51061 ų
Envelope volume envelope_volume57928 ų
Hydration-shell volume shell_volume23786 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg27.12
Envelope Rg envelope_rg20.00
Shape Rg shape_rg19.68
Total Rg total_rg20.60
Total atoms total_atoms2888
Residues n_residues363
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 dmax68.0
Rg (real space) rg_real20.78
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.9020e+07
I(0) uncertainty (real space) i0_real_error3.5610e+05
Rg (reciprocal space) rg_reciprocal20.80
I(0) (reciprocal space) i0_reciprocal29020000.0000
Solution quality estimate total_estimate0.6178
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7909000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)