7fc6

Crystal structure of SARS-CoV RBD and horse ACE2

Method: X-RAY DIFFRACTION Dmax: 105.3 Å Quality: REASONABLE

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

Angiotensin-converting enzyme

Equus caballus

UniProt F6V9L3

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–615 Not recorded Spike protein S1 × 1 (P59594) 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 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.03M Citric acid/0.07M BIS-TRIS propane pH7.6, 20% w/v polyethylene glycol 3350 Resolution 2.65 Å R-free 0.235

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F6V9L3_HORSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–597; UniProt 19–615

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain S; UniProt 321–512 Not recorded Angiotensin-converting enzyme × 1 (F6V9L3) 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 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.03M Citric acid/0.07M BIS-TRIS propane pH7.6, 20% w/v polyethylene glycol 3350 Resolution 2.65 Å R-free 0.235

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 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS
Isoform
PDB entities 2
Chains and sequence ranges Author chain S; PDBConstruct 1–192; UniProt 321–512

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 7fc6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7fc6
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7fc6
Deposition date deposition_date2021-07-13
Structure title titleCrystal structure of SARS-CoV RBD and horse ACE2
Keywords keywordsSARS, spike, receptor binding domain, horse, ACE2, VIRAL PROTEIN, VIRAL PROTEIN-PROTEIN BINDING complex; VIRAL PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.54
Radius of gyration Rg (electron density) rg_electron30.04
Forward intensity I(0) i0131211000.00
Molecular weight molecular_weight91437.0 kDa
Excluded volume excluded_volume114290 ų
Envelope volume envelope_volume141100 ų
Hydration-shell volume shell_volume39871 ų
Envelope diameter envelope_diameter113.1
Shell Rg shell_rg36.79
Envelope Rg envelope_rg30.05
Shape Rg shape_rg30.01
Total Rg total_rg30.72
Total atoms total_atoms6448
Residues n_residues789
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 dmax105.3
Rg (real space) rg_real30.62
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.3120e+08
I(0) uncertainty (real space) i0_real_error1.9380e+06
Rg (reciprocal space) rg_reciprocal30.59
I(0) (reciprocal space) i0_reciprocal131200000.0000
Solution quality estimate total_estimate0.6689
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis-0.048
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33640000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.970; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)