9uxs

The local refine of 3D reconstruction of the complex formed by SARS-CoV2 BA.1 spike glycoprotein and a single-domain antibody

Method: ELECTRON MICROSCOPY Dmax: 71.9 Å Quality: EXCELLENT

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

Spike glycoprotein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC2

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 14–1208 Not recorded single-domain antibody × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1188; UniProt 14–1208

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 9uxs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uxs
Deposition date deposition_date2025-05-14
Structure title titleThe local refine of 3D reconstruction of the complex formed by SARS-CoV2 BA.1 spike glycoprotein and a single-domain antibody
Keywords keywordsSARS-CoV2, RBD, Single-domain antibody, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.49
Radius of gyration Rg (electron density) rg_electron21.53
Forward intensity I(0) i022105700.00
Molecular weight molecular_weight36211.0 kDa
Excluded volume excluded_volume45446 ų
Envelope volume envelope_volume55852 ų
Hydration-shell volume shell_volume22045 ų
Envelope diameter envelope_diameter73.1
Shell Rg shell_rg27.86
Envelope Rg envelope_rg21.81
Shape Rg shape_rg21.49
Total Rg total_rg22.52
Total atoms total_atoms2559
Residues n_residues316
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 dmax71.9
Rg (real space) rg_real22.43
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.2110e+07
I(0) uncertainty (real space) i0_real_error2.9700e+05
Rg (reciprocal space) rg_reciprocal22.45
I(0) (reciprocal space) i0_reciprocal22110000.0000
Solution quality estimate total_estimate0.9043
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4417000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)