8hqy

Cryo-EM structure of SSX1 bound to the H2AK119Ub nucleosome at a resolution of 3.05 angstrom

Method: ELECTRON MICROSCOPY Dmax: 121.7 Å Quality: EXCELLENT

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

Histone H3

Homo sapiens

UniProt A0A653DHJ5

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 39–135 Chain E; UniProt 39–135 Not recorded Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H4 × 1 (A0A8C2GGI7) Histone H2A type 1-B/E × 1 (P04908) Protein SSX2 × 1 (Q16385) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A653DHJ5_CALMS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 39–135 Author chain E; PDBConstruct 1–97; UniProt 39–135

Histone H4 (Fragment)

Homo sapiens

UniProt A0A093PN76

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–83 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H4 × 1 (A0A8C2GGI7) Histone H2A type 1-B/E × 1 (P04908) Protein SSX2 × 1 (Q16385) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A093PN76_9PASS
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–83; UniProt 1–83

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 14–119 Chain G; UniProt 14–119 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2B type 1-K × 2 (O60814) Histone H4 × 1 (A0A8C2GGI7) Protein SSX2 × 1 (Q16385) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3, 6
Chains and sequence ranges Author chain C; PDBConstruct 1–106; UniProt 14–119 Author chain G; PDBConstruct 1–106; UniProt 14–119

Histone H2B type 1-K

Homo sapiens

UniProt O60814

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 35–125 Chain H; UniProt 35–125 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2A type 1-B/E × 1 (P04908) Histone H4 × 1 (A0A8C2GGI7) Histone H2A type 1-B/E × 1 (P04908) Protein SSX2 × 1 (Q16385) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–91; UniProt 35–125 Author chain H; PDBConstruct 1–91; UniProt 35–125

Histone H4

Homo sapiens

UniProt A0A8C2GGI7

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 11–91 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H2A type 1-B/E × 1 (P04908) Protein SSX2 × 1 (Q16385) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8C2GGI7_CYPCA
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–81; UniProt 11–91

Protein SSX2

Homo sapiens

UniProt Q16385

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain S; UniProt 162–184 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H4 × 1 (A0A8C2GGI7) Histone H2A type 1-B/E × 1 (P04908) Polyubiquitin-B (Fragment) × 1 (J3QS39) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name SSX2_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–23; UniProt 162–184

Polyubiquitin-B (Fragment)

Homo sapiens

UniProt J3QS39

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain U; UniProt 1–74 Not recorded Histone H3 × 2 (A0A653DHJ5) Histone H4 (Fragment) × 1 (A0A093PN76) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H4 × 1 (A0A8C2GGI7) Histone H2A type 1-B/E × 1 (P04908) Protein SSX2 × 1 (Q16385) DNA (137-MER) × 1 DNA (136-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

38 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name J3QS39_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–74; UniProt 1–74

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 8hqy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hqy
Deposition date deposition_date2022-12-14
Structure title titleCryo-EM structure of SSX1 bound to the H2AK119Ub nucleosome at a resolution of 3.05 angstrom
Keywords keywordsSSX1, H2AK119Ub nucleosome, Synovial Sarcoma, ssBAF, reader protein, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.26
Radius of gyration Rg (electron density) rg_electron37.66
Forward intensity I(0) i0831521000.00
Molecular weight molecular_weight179880.0 kDa
Excluded volume excluded_volume201800 ų
Envelope volume envelope_volume302340 ų
Hydration-shell volume shell_volume65063 ų
Envelope diameter envelope_diameter127.7
Shell Rg shell_rg45.38
Envelope Rg envelope_rg36.97
Shape Rg shape_rg37.48
Total Rg total_rg38.40
Total atoms total_atoms12301
Residues n_residues1119
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 dmax121.7
Rg (real space) rg_real40.07
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real8.3150e+08
I(0) uncertainty (real space) i0_real_error1.2900e+07
Rg (reciprocal space) rg_reciprocal40.26
I(0) (reciprocal space) i0_reciprocal831700000.0000
Solution quality estimate total_estimate0.9033
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.599
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48750000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)