7y3n

Crystal structure of SARS-CoV receptor binding domain in complex with human antibody BIOLS56

Method: X-RAY DIFFRACTION Dmax: 138.6 Å Quality: GOOD

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

Spike protein S1

Severe acute respiratory syndrome coronavirus

UniProt P59594

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 306–527 Fragment:receptor binding domain Heavy chain of BIOLS56 × 1 Light chain of BIOLS56 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;291 K;20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000 Resolution 2.97 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 306–527 Fragment:receptor binding domain Heavy chain of BIOLS56 × 1 Light chain of BIOLS56 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;291 K;20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000 Resolution 2.97 Å R-free 0.263
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 306–527 Fragment:receptor binding domain Heavy chain of BIOLS56 × 1 Light chain of BIOLS56 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;291 K;20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000 Resolution 2.97 Å R-free 0.263

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.

76 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–222; UniProt 306–527 Author chain B; PDBConstruct 1–222; UniProt 306–527 Author chain E; PDBConstruct 1–222; UniProt 306–527

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 7y3n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7y3n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7y3n
Deposition date deposition_date2022-06-11
Structure title titleCrystal structure of SARS-CoV receptor binding domain in complex with human antibody BIOLS56
Keywords keywordsSARS-CoV, antibody, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.35
Radius of gyration Rg (electron density) rg_electron43.90
Forward intensity I(0) i0636249000.00
Molecular weight molecular_weight207450.0 kDa
Excluded volume excluded_volume259140 ų
Envelope volume envelope_volume370930 ų
Hydration-shell volume shell_volume70098 ų
Envelope diameter envelope_diameter143.4
Shell Rg shell_rg49.52
Envelope Rg envelope_rg42.56
Shape Rg shape_rg43.90
Total Rg total_rg44.17
Total atoms total_atoms14620
Residues n_residues1890
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 dmax138.6
Rg (real space) rg_real44.11
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real6.3620e+08
I(0) uncertainty (real space) i0_real_error1.0910e+07
Rg (reciprocal space) rg_reciprocal44.35
I(0) (reciprocal space) i0_reciprocal636400000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.6
Skewness Skewness skewness0.079
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53050000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.843

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)