7efp

Structure of SARS-CoV-2 spike receptor-binding domain in complex with high affinity ACE2 mutant (S19W,N330Y)

Method: X-RAY DIFFRACTION Dmax: 105.2 Å Quality: GOOD

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

Processed angiotensin-converting enzyme 2

Homo sapiens

UniProt Q9BYF1

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 19–615 Mutation:S19W, N330Y Spike glycoprotein × 1 (P0DTC2) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;1.6 M Ammonium sulfate, 0.1 M MES pH6.5, 10 % v/v 1,4-Dioxane Resolution 2.70 Å R-free 0.224

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.

338 other PDB entries and 388 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–599; UniProt 19–615

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 320–537 Fragment:UNP 320-537 Processed angiotensin-converting enzyme 2 × 1 (Q9BYF1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;1.6 M Ammonium sulfate, 0.1 M MES pH6.5, 10 % v/v 1,4-Dioxane Resolution 2.70 Å R-free 0.224

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 1–218; UniProt 320–537

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 7efp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7efp
Deposition date deposition_date2021-03-22
Structure title titleStructure of SARS-CoV-2 spike receptor-binding domain in complex with high affinity ACE2 mutant (S19W,N330Y)
Keywords keywordsreceptor-binding domain, angiotensin converting enzyme 2, 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_guinier30.67
Radius of gyration Rg (electron density) rg_electron30.17
Forward intensity I(0) i0131476000.00
Molecular weight molecular_weight91643.0 kDa
Excluded volume excluded_volume114570 ų
Envelope volume envelope_volume140260 ų
Hydration-shell volume shell_volume39563 ų
Envelope diameter envelope_diameter111.2
Shell Rg shell_rg36.73
Envelope Rg envelope_rg30.23
Shape Rg shape_rg30.14
Total Rg total_rg30.82
Total atoms total_atoms6522
Residues n_residues790
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 dmax105.2
Rg (real space) rg_real30.75
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.3150e+08
I(0) uncertainty (real space) i0_real_error2.1180e+06
Rg (reciprocal space) rg_reciprocal30.72
I(0) (reciprocal space) i0_reciprocal131500000.0000
Solution quality estimate total_estimate0.8586
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.492
Kurtosis Kurtosis kurtosis-0.076
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29900000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)