5wg6

Human Polycomb Repressive Complex 2 in complex with GSK126 inhibitor

Method: X-RAY DIFFRACTION Dmax: 126.2 Å Quality: GOOD

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

Histone-lysine N-methyltransferase EZH2,Polycomb protein SUZ12 (E.C.2.1.1.43) chimera

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 543–695 Not recorded Polycomb protein EED × 1 (O75530) ZN ZINC ION × 8 A9G 1-[(2S)-butan-2-yl]-N-[(4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl]-3-methyl-6-[6-(piperazin-1-yl)pyridin-3-yl]-1H-indole-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 543–695 Not recorded Polycomb protein EED × 1 (O75530) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300

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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUZ12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 707–859; UniProt 543–695 Author chain C; PDBConstruct 707–859; UniProt 543–695

Histone-lysine N-methyltransferase EZH2,Polycomb protein SUZ12 (E.C.2.1.1.43) chimera

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–182 Chain A; UniProt 196–385 Chain A; UniProt 421–746 Not recorded Polycomb protein EED × 1 (O75530) ZN ZINC ION × 8 A9G 1-[(2S)-butan-2-yl]-N-[(4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl]-3-methyl-6-[6-(piperazin-1-yl)pyridin-3-yl]-1H-indole-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–182 Chain C; UniProt 196–385 Chain C; UniProt 421–746 Not recorded Polycomb protein EED × 1 (O75530) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300

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 1
Chains and sequence ranges Author chain A; PDBConstruct 10–190; UniProt 2–182 Author chain A; PDBConstruct 191–380; UniProt 196–385 Author chain A; PDBConstruct 381–706; UniProt 421–746 Author chain C; PDBConstruct 10–190; UniProt 2–182 Author chain C; PDBConstruct 191–380; UniProt 196–385 Author chain C; PDBConstruct 381–706; UniProt 421–746

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–441 Not recorded Histone-lysine N-methyltransferase EZH2,Polycomb protein SUZ12 (E.C.2.1.1.43) chimera × 1 (Q15910,Q15022) ZN ZINC ION × 8 A9G 1-[(2S)-butan-2-yl]-N-[(4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl]-3-methyl-6-[6-(piperazin-1-yl)pyridin-3-yl]-1H-indole-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–441 Not recorded Histone-lysine N-methyltransferase EZH2,Polycomb protein SUZ12 (E.C.2.1.1.43) chimera × 1 (Q15910,Q15022) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;200 mM ammonium citrate pH 7.2, 16% PEG 3350 Resolution 3.90 Å R-free 0.300

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 2
Chains and sequence ranges Author chain B; PDBConstruct 3–442; UniProt 2–441 Author chain D; PDBConstruct 3–442; UniProt 2–441

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 5wg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wg6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wg6
Deposition date deposition_date2017-07-13
Structure title titleHuman Polycomb Repressive Complex 2 in complex with GSK126 inhibitor
Keywords keywordscomplex, epigenetics, transferase, 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_guinier41.08
Radius of gyration Rg (electron density) rg_electron40.37
Forward intensity I(0) i0594210000.00
Molecular weight molecular_weight193120.0 kDa
Excluded volume excluded_volume238710 ų
Envelope volume envelope_volume333260 ų
Hydration-shell volume shell_volume67273 ų
Envelope diameter envelope_diameter134.5
Shell Rg shell_rg47.35
Envelope Rg envelope_rg39.64
Shape Rg shape_rg40.32
Total Rg total_rg40.89
Total atoms total_atoms13474
Residues n_residues1650
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 dmax126.2
Rg (real space) rg_real40.89
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real5.9420e+08
I(0) uncertainty (real space) i0_real_error1.0420e+07
Rg (reciprocal space) rg_reciprocal41.08
I(0) (reciprocal space) i0_reciprocal594300000.0000
Solution quality estimate total_estimate0.8999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.5
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.578
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87150000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)