7wsh

Cryo-EM structure of SARS-CoV-2 spike receptor-binding domain in complex with sea lion ACE2

Method: ELECTRON MICROSCOPY Dmax: 108.9 Å Quality: GOOD

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

Angiotensin-converting enzyme

Mammalia

UniProt A0A6J2EID0

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 1–806 Not recorded Spike protein S1 × 1 (P0DTC2) ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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 A0A6J2EID0_ZALCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–806; UniProt 1–806

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 B; UniProt 333–527 Not recorded Angiotensin-converting enzyme × 1 (A0A6J2EID0) ZN ZINC ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–195; UniProt 333–527

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 7wsh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7wsh
Deposition date deposition_date2022-01-29
Structure title titleCryo-EM structure of SARS-CoV-2 spike receptor-binding domain in complex with sea lion ACE2
Keywords keywordscomplex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.33
Radius of gyration Rg (electron density) rg_electron30.86
Forward intensity I(0) i0133517000.00
Molecular weight molecular_weight91567.0 kDa
Excluded volume excluded_volume114070 ų
Envelope volume envelope_volume142540 ų
Hydration-shell volume shell_volume39387 ų
Envelope diameter envelope_diameter118.5
Shell Rg shell_rg37.35
Envelope Rg envelope_rg31.03
Shape Rg shape_rg30.83
Total Rg total_rg31.49
Total atoms total_atoms6457
Residues n_residues793
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 dmax108.9
Rg (real space) rg_real31.44
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.3350e+08
I(0) uncertainty (real space) i0_real_error2.0950e+06
Rg (reciprocal space) rg_reciprocal31.39
I(0) (reciprocal space) i0_reciprocal133500000.0000
Solution quality estimate total_estimate0.8463
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.524
Kurtosis Kurtosis kurtosis0.046
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29480000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.725; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)