7qe0

80S-bound human SKI complex in the open state

Method: ELECTRON MICROSCOPY Dmax: 117.2 Å Quality: GOOD

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

Helicase SKI2W

Homo sapiens

UniProt Q15477

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 A; UniProt 1–1246 Not recorded ;RNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*UP*U)-3') ; × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.50 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKIV2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1246; UniProt 1–1246

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 7qe0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qe0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qe0
Deposition date deposition_date2021-12-01
Structure title title80S-bound human SKI complex in the open state
Keywords keywordsmultiprotein complex, RNA helicase, DExH-box helicase, ATPase, RNA binding, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.63
Radius of gyration Rg (electron density) rg_electron37.49
Forward intensity I(0) i0186643000.00
Molecular weight molecular_weight108670.0 kDa
Excluded volume excluded_volume135790 ų
Envelope volume envelope_volume201590 ų
Hydration-shell volume shell_volume45732 ų
Envelope diameter envelope_diameter117.4
Shell Rg shell_rg42.65
Envelope Rg envelope_rg36.76
Shape Rg shape_rg37.50
Total Rg total_rg37.82
Total atoms total_atoms7618
Residues n_residues958
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 dmax117.2
Rg (real space) rg_real37.70
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.8660e+08
I(0) uncertainty (real space) i0_real_error2.9480e+06
Rg (reciprocal space) rg_reciprocal37.66
I(0) (reciprocal space) i0_reciprocal186600000.0000
Solution quality estimate total_estimate0.8615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.686
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37220000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.352

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)