6xdc

Cryo-EM structure of SARS-CoV-2 ORF3a

Method: ELECTRON MICROSCOPY Dmax: 83.4 Å Quality: GOOD

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

ORF3a protein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC3

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–275 Chain B; UniProt 1–275 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;1 blot force, 5 second wait time, 3 second blot time Resolution 2.90 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.

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

View Construct and Data Evidence
UniProt name AP3A_SARS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–275; UniProt 1–275 Author chain B; PDBConstruct 1–275; UniProt 1–275

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 6xdc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xdc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xdc
Deposition date deposition_date2020-06-10
Structure title titleCryo-EM structure of SARS-CoV-2 ORF3a
Keywords keywordsSARS-CoV-2, coronavirus, viroporin, ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier24.61
Radius of gyration Rg (electron density) rg_electron24.38
Forward intensity I(0) i028248000.00
Molecular weight molecular_weight44476.0 kDa
Excluded volume excluded_volume57149 ų
Envelope volume envelope_volume70096 ų
Hydration-shell volume shell_volume25126 ų
Envelope diameter envelope_diameter85.3
Shell Rg shell_rg30.38
Envelope Rg envelope_rg24.37
Shape Rg shape_rg24.41
Total Rg total_rg25.08
Total atoms total_atoms3150
Residues n_residues386
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 dmax83.4
Rg (real space) rg_real24.75
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.8250e+07
I(0) uncertainty (real space) i0_real_error4.1910e+05
Rg (reciprocal space) rg_reciprocal24.72
I(0) (reciprocal space) i0_reciprocal28250000.0000
Solution quality estimate total_estimate0.8613
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis-0.135
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5973000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)