8equ

Structure of SARS-CoV-2 Orf3a in late endosome/lysosome-like environment, Saposin A nanodisc

Method: ELECTRON MICROSCOPY Dmax: 87.0 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–275 Chain B; UniProt 1–275 Not recorded Saposin-A × 2 (P07602) Saposin A, polyalanine model × 4 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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

Saposin-A

Homo sapiens

UniProt P07602

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 60–140 Chain F; UniProt 60–140 Not recorded ORF3a protein × 2 (P0DTC3) Saposin A, polyalanine model × 4 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 26–106; UniProt 60–140 Author chain F; PDBConstruct 26–106; UniProt 60–140

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 8equ

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8equ
Deposition date deposition_date2022-10-09
最后修订 last_revision2023-02-08
Structure title titleStructure of SARS-CoV-2 Orf3a in late endosome/lysosome-like environment, Saposin A nanodisc
Keywords keywordsMembrane protein, SARS-CoV-2, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.38
Radius of gyration Rg (electron density) rg_electron29.52
Forward intensity I(0) i0115144000.00
Molecular weight molecular_weight81563.0 kDa
Excluded volume excluded_volume101160 ų
Envelope volume envelope_volume164780 ų
Hydration-shell volume shell_volume45369 ų
Envelope diameter envelope_diameter86.9
Shell Rg shell_rg37.98
Envelope Rg envelope_rg28.82
Shape Rg shape_rg29.60
Total Rg total_rg30.26
Total atoms total_atoms5764
Residues n_residues858
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 dmax87.0
Rg (real space) rg_real31.11
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.1510e+08
I(0) uncertainty (real space) i0_real_error1.5230e+06
Rg (reciprocal space) rg_reciprocal31.23
I(0) (reciprocal space) i0_reciprocal115200000.0000
Solution quality estimate total_estimate0.6909
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.0
Skewness Skewness skewness-0.007
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8370000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.992; Stabil: 1.000; Sysdev: 0.169; Positv: 1.000; Valcen: 0.995; Smooth: 0.500

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)