9xzi

Crystal Structure of the SUZ12-RBBP4-PHF19-EPOP PRC2.1 Subcomplex

Method: X-RAY DIFFRACTION Dmax: 105.6 Å Quality: GOOD

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

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 76–545 Fragment:residues 76-545 Histone-binding protein RBBP4 × 2 (Q09028) PHD finger protein 19 × 2 (Q5T6S3) Elongin BC and Polycomb repressive complex 2-associated protein × 2 (A6NHQ4) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium Citrate, Sodium Acetate, PEG 4000 Resolution 2.69 Å R-free 0.253

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 1
Chains and sequence ranges Author chain A; PDBConstruct 4–473; UniProt 76–545

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–425 Not recorded Polycomb protein SUZ12 × 2 (Q15022) PHD finger protein 19 × 2 (Q5T6S3) Elongin BC and Polycomb repressive complex 2-associated protein × 2 (A6NHQ4) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium Citrate, Sodium Acetate, PEG 4000 Resolution 2.69 Å R-free 0.253

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 B; PDBConstruct 20–444; UniProt 1–425

PHD finger protein 19

Homo sapiens

UniProt Q5T6S3

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 531–580 Fragment:residues 531-580 Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 2 (Q09028) Elongin BC and Polycomb repressive complex 2-associated protein × 2 (A6NHQ4) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium Citrate, Sodium Acetate, PEG 4000 Resolution 2.69 Å R-free 0.253

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF19_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–53; UniProt 531–580

Elongin BC and Polycomb repressive complex 2-associated protein

Homo sapiens

UniProt A6NHQ4

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 311–379 Fragment:residues 311-379 Polycomb protein SUZ12 × 2 (Q15022) Histone-binding protein RBBP4 × 2 (Q09028) PHD finger protein 19 × 2 (Q5T6S3) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Sodium Citrate, Sodium Acetate, PEG 4000 Resolution 2.69 Å R-free 0.253

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPOP_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–70; UniProt 311–379

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 9xzi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xzi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xzi
Deposition date deposition_date2025-08-27
Structure title titleCrystal Structure of the SUZ12-RBBP4-PHF19-EPOP PRC2.1 Subcomplex
Keywords keywordsmethyltransferase, transcription, epigenetics; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.22
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i0121283000.00
Molecular weight molecular_weight87446.0 kDa
Excluded volume excluded_volume109310 ų
Envelope volume envelope_volume146950 ų
Hydration-shell volume shell_volume37976 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg38.90
Envelope Rg envelope_rg33.07
Shape Rg shape_rg32.82
Total Rg total_rg33.42
Total atoms total_atoms6163
Residues n_residues763
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 dmax105.6
Rg (real space) rg_real33.24
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real1.2130e+08
I(0) uncertainty (real space) i0_real_error1.8510e+06
Rg (reciprocal space) rg_reciprocal33.24
I(0) (reciprocal space) i0_reciprocal121300000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.655
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26360000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.875

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)