8rao

Structure of Sen1-ADP.BeF3-RNA complex

Method: ELECTRON MICROSCOPY Dmax: 89.4 Å Quality: GOOD

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

Helicase SEN1

Saccharomyces cerevisiae

UniProt Q00416

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain O; UniProt 1–2231 Not recorded RNA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

9 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEN1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain O; PDBConstruct 1–2231; UniProt 1–2231

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 8rao

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rao
Deposition date deposition_date2023-12-01
Structure title titleStructure of Sen1-ADP.BeF3-RNA complex
Keywords keywordsRNA Polymerase II, Pol II, termination, Sen1, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.06
Radius of gyration Rg (electron density) rg_electron27.26
Forward intensity I(0) i0116731000.00
Molecular weight molecular_weight82545.0 kDa
Excluded volume excluded_volume102260 ų
Envelope volume envelope_volume126310 ų
Hydration-shell volume shell_volume37441 ų
Envelope diameter envelope_diameter98.2
Shell Rg shell_rg35.49
Envelope Rg envelope_rg27.70
Shape Rg shape_rg27.29
Total Rg total_rg27.94
Total atoms total_atoms5781
Residues n_residues703
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 dmax89.4
Rg (real space) rg_real27.95
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.1670e+08
I(0) uncertainty (real space) i0_real_error1.6770e+06
Rg (reciprocal space) rg_reciprocal27.99
I(0) (reciprocal space) i0_reciprocal116700000.0000
Solution quality estimate total_estimate0.8203
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21700000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)