7c8k

Structural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2

Method: ELECTRON MICROSCOPY Dmax: 79.4 Å Quality: EXCELLENT

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

Angiotensin-converting enzyme

Rhinolophus macrotis

UniProt E2DHI3

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–614 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E2DHI3_RHIMR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–596; UniProt 19–614

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 7c8k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7c8k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7c8k
Deposition date deposition_date2020-06-02
Structure title titleStructural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2
Keywords keywordsCOVID-19, receptor binding domain (RBD), Rhinolophus macrotis, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.14
Radius of gyration Rg (electron density) rg_electron24.91
Forward intensity I(0) i077377400.00
Molecular weight molecular_weight68865.0 kDa
Excluded volume excluded_volume86000 ų
Envelope volume envelope_volume106830 ų
Hydration-shell volume shell_volume34567 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg33.30
Envelope Rg envelope_rg24.73
Shape Rg shape_rg24.89
Total Rg total_rg25.86
Total atoms total_atoms4853
Residues n_residues596
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 dmax79.4
Rg (real space) rg_real25.95
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real7.7380e+07
I(0) uncertainty (real space) i0_real_error8.8680e+05
Rg (reciprocal space) rg_reciprocal26.01
I(0) (reciprocal space) i0_reciprocal77380000.0000
Solution quality estimate total_estimate0.9009
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.059
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16730000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)