9xyc

Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome LEDGF+nucleosome map Q

Method: ELECTRON MICROSCOPY Dmax: 138.6 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain a; UniProt 1–136 Chain e; UniProt 1–136 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (139-MER) × 1 DNA (139-MER) × 1 Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) PC4 and SFRS1-interacting protein × 1 (O75475) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain a; PDBConstruct 1–136; UniProt 1–136 Author chain e; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis

UniProt P62799

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain b; UniProt 1–103 Chain f; UniProt 1–103 Not recorded DNA (139-MER) × 1 DNA (139-MER) × 1 Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) PC4 and SFRS1-interacting protein × 1 (O75475) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain b; PDBConstruct 1–103; UniProt 1–103 Author chain f; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain c; UniProt 1–130 Chain g; UniProt 1–130 Not recorded DNA (139-MER) × 1 DNA (139-MER) × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) PC4 and SFRS1-interacting protein × 1 (O75475) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 5
Chains and sequence ranges Author chain c; PDBConstruct 1–130; UniProt 1–130 Author chain g; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain d; UniProt 1–126 Chain h; UniProt 1–126 Not recorded DNA (139-MER) × 1 DNA (139-MER) × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) PC4 and SFRS1-interacting protein × 1 (O75475) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 6
Chains and sequence ranges Author chain d; PDBConstruct 1–126; UniProt 1–126 Author chain h; PDBConstruct 1–126; UniProt 1–126

PC4 and SFRS1-interacting protein

Homo sapiens

UniProt O75475

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain l; UniProt 2–530 Not recorded DNA (139-MER) × 1 DNA (139-MER) × 1 Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

34 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSIP1_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain l; PDBConstruct 4–532; UniProt 2–530

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 9xyc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xyc
Deposition date deposition_date2025-08-25
Structure title titlePol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome LEDGF+nucleosome map Q
Keywords keywordspolymerase, elongation factor, nucleosome, TRANSCRIPTION, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.73
Radius of gyration Rg (electron density) rg_electron39.79
Forward intensity I(0) i0854594000.00
Molecular weight molecular_weight182720.0 kDa
Excluded volume excluded_volume204950 ų
Envelope volume envelope_volume307970 ų
Hydration-shell volume shell_volume64258 ų
Envelope diameter envelope_diameter136.0
Shell Rg shell_rg45.83
Envelope Rg envelope_rg39.28
Shape Rg shape_rg39.68
Total Rg total_rg40.29
Total atoms total_atoms12505
Residues n_residues1130
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 dmax138.6
Rg (real space) rg_real41.64
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real8.5460e+08
I(0) uncertainty (real space) i0_real_error1.3300e+07
Rg (reciprocal space) rg_reciprocal41.73
I(0) (reciprocal space) i0_reciprocal854700000.0000
Solution quality estimate total_estimate0.8863
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.4
Skewness Skewness skewness0.241
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60130000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)