8q93

Crystal structure of the SARS-COV-2 RBD with neutralizing-VHHs Re30H02 and Re21D01

Method: X-RAY DIFFRACTION Dmax: 87.8 Å Quality: GOOD

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

Spike protein S1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 334–526 Not recorded Nanobody Re21D01 × 1 Nanobody Re30H02 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;28% PEG smear broad, 50 mM arginine, 50 mM MSG, 5% Glycerol Resolution 3.10 Å R-free 0.257

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 1
Chains and sequence ranges Author chain A; PDBConstruct 4–196; UniProt 334–526

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 8q93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q93
Deposition date deposition_date2023-08-19
Structure title titleCrystal structure of the SARS-COV-2 RBD with neutralizing-VHHs Re30H02 and Re21D01
Keywords keywordsNeutralizing VHH, Fold-promoter, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.46
Radius of gyration Rg (electron density) rg_electron24.68
Forward intensity I(0) i039729900.00
Molecular weight molecular_weight47695.0 kDa
Excluded volume excluded_volume59074 ų
Envelope volume envelope_volume72941 ų
Hydration-shell volume shell_volume25312 ų
Envelope diameter envelope_diameter91.8
Shell Rg shell_rg31.23
Envelope Rg envelope_rg24.82
Shape Rg shape_rg24.62
Total Rg total_rg25.59
Total atoms total_atoms3360
Residues n_residues438
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 dmax87.8
Rg (real space) rg_real25.49
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real3.9730e+07
I(0) uncertainty (real space) i0_real_error5.8780e+05
Rg (reciprocal space) rg_reciprocal25.48
I(0) (reciprocal space) i0_reciprocal39730000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10930000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)