8rj7

The crystal structure of the SARS-CoV-2 receptor binding domain in complex with the neutralizing nanobody 1.29

Method: X-RAY DIFFRACTION Dmax: 128.7 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 332–528 Not recorded Camel-derived nanobody 1.29 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% PEG-3350, 100mM Bicine pH 9, 20 mM (NH4)2SO4 Resolution 2.10 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 332–528 Not recorded Camel-derived nanobody 1.29 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 LYS LYSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% PEG-3350, 100mM Bicine pH 9, 20 mM (NH4)2SO4 Resolution 2.10 Å R-free 0.222
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 332–528 Not recorded Camel-derived nanobody 1.29 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% PEG-3350, 100mM Bicine pH 9, 20 mM (NH4)2SO4 Resolution 2.10 Å R-free 0.222
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 332–528 Not recorded Camel-derived nanobody 1.29 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% PEG-3350, 100mM Bicine pH 9, 20 mM (NH4)2SO4 Resolution 2.10 Å R-free 0.222
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 332–528 Not recorded Camel-derived nanobody 1.29 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;15% PEG-3350, 100mM Bicine pH 9, 20 mM (NH4)2SO4 Resolution 2.10 Å R-free 0.222

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 2469 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 3–199; UniProt 332–528 Author chain C; PDBConstruct 3–199; UniProt 332–528 Author chain E; PDBConstruct 3–199; UniProt 332–528 Author chain G; PDBConstruct 3–199; UniProt 332–528 Author chain I; PDBConstruct 3–199; UniProt 332–528

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 8rj7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rj7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rj7
Deposition date deposition_date2023-12-20
最后修订 last_revision2024-11-27
Structure title titleThe crystal structure of the SARS-CoV-2 receptor binding domain in complex with the neutralizing nanobody 1.29
Keywords keywordscoronavirus, COVID-19, RBD, SARS-CoV-2, spike, nanobodies, neutralization, VIRAL PROTEIN, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.75
Radius of gyration Rg (electron density) rg_electron38.53
Forward intensity I(0) i0472558000.00
Molecular weight molecular_weight173630.0 kDa
Excluded volume excluded_volume215310 ų
Envelope volume envelope_volume284260 ų
Hydration-shell volume shell_volume61525 ų
Envelope diameter envelope_diameter138.5
Shell Rg shell_rg44.36
Envelope Rg envelope_rg38.28
Shape Rg shape_rg38.48
Total Rg total_rg39.00
Total atoms total_atoms12248
Residues n_residues1574
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 dmax128.7
Rg (real space) rg_real38.70
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real4.7260e+08
I(0) uncertainty (real space) i0_real_error8.3070e+06
Rg (reciprocal space) rg_reciprocal38.73
I(0) (reciprocal space) i0_reciprocal472600000.0000
Solution quality estimate total_estimate0.8692
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.2
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.171
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67000000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)