7a95

SARS-CoV-2 Spike Glycoprotein with 1 ACE2 Bound and 1 RBD Erect in Clockwise Direction

Method: ELECTRON MICROSCOPY Dmax: 205.5 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1208 Chain B; UniProt 1–1208 Chain C; UniProt 1–1208 Not recorded Angiotensin-converting enzyme 2 × 1 (Q9BYF1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

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 32–1239; UniProt 1–1208 Author chain B; PDBConstruct 32–1239; UniProt 1–1208 Author chain C; PDBConstruct 32–1239; UniProt 1–1208

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 19–615 Not recorded Spike glycoprotein × 3 (P0DTC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

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 2
Chains and sequence ranges Author chain D; PDBConstruct 21–617; UniProt 19–615

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 7a95

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7a95
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7a95
Deposition date deposition_date2020-09-01
Structure title titleSARS-CoV-2 Spike Glycoprotein with 1 ACE2 Bound and 1 RBD Erect in Clockwise Direction
Keywords keywordsSARS-CoV-2, Spike, Virus Glycoprotein, Coronavirus, VIRAL PROTEIN, ACE2; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.69
Radius of gyration Rg (electron density) rg_electron64.06
Forward intensity I(0) i02495440000.00
Molecular weight molecular_weight423870.0 kDa
Excluded volume excluded_volume531530 ų
Envelope volume envelope_volume853590 ų
Hydration-shell volume shell_volume117410 ų
Envelope diameter envelope_diameter234.1
Shell Rg shell_rg61.00
Envelope Rg envelope_rg61.98
Shape Rg shape_rg64.11
Total Rg total_rg63.80
Total atoms total_atoms29887
Residues n_residues3794
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 dmax205.5
Rg (real space) rg_real63.88
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real2.4930e+09
I(0) uncertainty (real space) i0_real_error4.6560e+07
Rg (reciprocal space) rg_reciprocal63.35
I(0) (reciprocal space) i0_reciprocal2492000000.0000
Solution quality estimate total_estimate0.8553
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary74.0
Skewness Skewness skewness0.484
Kurtosis Kurtosis kurtosis-0.100
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0046
Highest regularization parameter α highest_alpha203200000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.389

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)