7det

Crystal structure of SARS-CoV-2 RBD in complex with a neutralizing antibody scFv

Method: X-RAY DIFFRACTION Dmax: 118.3 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 334–530 Fragment:RBD antibody scFv × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2M sodium chloride, 0.1M Tris pH 8.5, 29% w/v Polyethylene glycol 3350 Resolution 2.20 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 334–530 Fragment:RBD antibody scFv × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2M sodium chloride, 0.1M Tris pH 8.5, 29% w/v Polyethylene glycol 3350 Resolution 2.20 Å R-free 0.260

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 2472 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 1–197; UniProt 334–530 Author chain C; PDBConstruct 1–197; UniProt 334–530

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 7det

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7det
Deposition date deposition_date2020-11-05
Structure title titleCrystal structure of SARS-CoV-2 RBD in complex with a neutralizing antibody scFv
Keywords keywordsSARS-CoV-2, RBD, antibody, VIRAL PROTEIN, ANTIVIRAL PROTEIN, VIRAL PROTEIN-ANTIVIRAL PROTEIN complex; VIRAL PROTEIN/ANTIVIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.31
Radius of gyration Rg (electron density) rg_electron35.24
Forward intensity I(0) i0142000000.00
Molecular weight molecular_weight94748.0 kDa
Excluded volume excluded_volume117970 ų
Envelope volume envelope_volume155340 ų
Hydration-shell volume shell_volume37857 ų
Envelope diameter envelope_diameter127.8
Shell Rg shell_rg40.24
Envelope Rg envelope_rg34.83
Shape Rg shape_rg35.18
Total Rg total_rg35.79
Total atoms total_atoms6686
Residues n_residues849
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 dmax118.3
Rg (real space) rg_real35.43
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real1.4200e+08
I(0) uncertainty (real space) i0_real_error2.5280e+06
Rg (reciprocal space) rg_reciprocal35.36
I(0) (reciprocal space) i0_reciprocal142000000.0000
Solution quality estimate total_estimate0.8614
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15950000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.570

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd7deta_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.318 — SARS receptor-binding domain-like
Superfamily Superfamily superfamilyd.318.1 — SARS receptor-binding domain-like
Family Family familyd.318.1.1 — SARS receptor-binding domain-like
Domain ID domain_idd7detb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7detb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7detc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.318 — SARS receptor-binding domain-like
Superfamily Superfamily superfamilyd.318.1 — SARS receptor-binding domain-like
Family Family familyd.318.1.1 — SARS receptor-binding domain-like
Domain ID domain_idd7detd1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7detd2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)