9yol

Tra1 module of ctSAGA

Method: ELECTRON MICROSCOPY Dmax: 202.2 Å Quality: GOOD

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

SCA7 domain-containing protein

OrganismNot specified

UniProt G0S6A1

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Q; UniProt 1–1273 Not recorded Spt20-like SEP domain-containing protein × 1 (G0RYM2) Chains: C × 1 (G0S660) Putative transcriptional coactivator HFI1 protein × 1 (G0SED0) Transcription initiation factor TFIID subunit 12 × 1 (G0S2A1) Non-specific serine/threonine protein kinase × 1 (G0S842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S6A1_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain Q; PDBConstruct 1–1273; UniProt 1–1273

Spt20-like SEP domain-containing protein

OrganismNot specified

UniProt G0RYM2

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–1192 Not recorded SCA7 domain-containing protein × 1 (G0S6A1) Chains: C × 1 (G0S660) Putative transcriptional coactivator HFI1 protein × 1 (G0SED0) Transcription initiation factor TFIID subunit 12 × 1 (G0S2A1) Non-specific serine/threonine protein kinase × 1 (G0S842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYM2_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1192; UniProt 1–1192

Chains: C

OrganismNot specified

UniProt G0S660

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–433 Not recorded SCA7 domain-containing protein × 1 (G0S6A1) Spt20-like SEP domain-containing protein × 1 (G0RYM2) Putative transcriptional coactivator HFI1 protein × 1 (G0SED0) Transcription initiation factor TFIID subunit 12 × 1 (G0S2A1) Non-specific serine/threonine protein kinase × 1 (G0S842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S660_CHATD
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–433; UniProt 1–433

Putative transcriptional coactivator HFI1 protein

OrganismNot specified

UniProt G0SED0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 1–485 Not recorded SCA7 domain-containing protein × 1 (G0S6A1) Spt20-like SEP domain-containing protein × 1 (G0RYM2) Chains: C × 1 (G0S660) Transcription initiation factor TFIID subunit 12 × 1 (G0S2A1) Non-specific serine/threonine protein kinase × 1 (G0S842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 G0SED0_CHATD
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–485; UniProt 1–485

Transcription initiation factor TFIID subunit 12

OrganismNot specified

UniProt G0S2A1

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain I; UniProt 1–770 Not recorded SCA7 domain-containing protein × 1 (G0S6A1) Spt20-like SEP domain-containing protein × 1 (G0RYM2) Chains: C × 1 (G0S660) Putative transcriptional coactivator HFI1 protein × 1 (G0SED0) Non-specific serine/threonine protein kinase × 1 (G0S842) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S2A1_CHATD
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–770; UniProt 1–770

Non-specific serine/threonine protein kinase

OrganismNot specified

UniProt G0S842

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–3893 Not recorded SCA7 domain-containing protein × 1 (G0S6A1) Spt20-like SEP domain-containing protein × 1 (G0RYM2) Chains: C × 1 (G0S660) Putative transcriptional coactivator HFI1 protein × 1 (G0SED0) Transcription initiation factor TFIID subunit 12 × 1 (G0S2A1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S842_CHATD
Isoform
PDB entities 6
Chains and sequence ranges Author chain A; PDBConstruct 1–3893; UniProt 1–3893

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 9yol

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yol
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9yol
Deposition date deposition_date2025-10-13
Structure title titleTra1 module of ctSAGA
Keywords keywordsctSAGA complex, Histone Acetyl Transferase (HAT) Module, Tra1 module and Core module, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.74
Radius of gyration Rg (electron density) rg_electron60.62
Forward intensity I(0) i02671750000.00
Molecular weight molecular_weight446890.0 kDa
Excluded volume excluded_volume564180 ų
Envelope volume envelope_volume892510 ų
Hydration-shell volume shell_volume120490 ų
Envelope diameter envelope_diameter204.0
Shell Rg shell_rg65.21
Envelope Rg envelope_rg58.82
Shape Rg shape_rg60.61
Total Rg total_rg60.79
Total atoms total_atoms62724
Residues n_residues3884
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 dmax202.2
Rg (real space) rg_real60.75
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real2.6720e+09
I(0) uncertainty (real space) i0_real_error5.8710e+07
Rg (reciprocal space) rg_reciprocal60.71
I(0) (reciprocal space) i0_reciprocal2671000000.0000
Solution quality estimate total_estimate0.8623
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.0
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha246800000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.504

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)