8h15

Structure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Closed Conformation

Method: ELECTRON MICROSCOPY Dmax: 155.1 Å Quality: GOOD

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

Spike glycoprotein

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 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 15–1193 Chain B; UniProt 15–1193 Chain C; UniProt 15–1193 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 5.54;Gibco PBS C10010 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 5–1183; UniProt 15–1193 Author chain B; PDBConstruct 5–1183; UniProt 15–1193 Author chain C; PDBConstruct 5–1183; UniProt 15–1193

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 8h15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8h15
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8h15
Deposition date deposition_date2022-09-30
Structure title titleStructure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Closed Conformation
Keywords keywordsPROTEIN ENGINEERING, SPIKE PROTEIN, SARS-COV-1, SARS-COV, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.73
Radius of gyration Rg (electron density) rg_electron47.41
Forward intensity I(0) i01475440000.00
Molecular weight molecular_weight323950.0 kDa
Excluded volume excluded_volume406920 ų
Envelope volume envelope_volume582390 ų
Hydration-shell volume shell_volume99396 ų
Envelope diameter envelope_diameter153.1
Shell Rg shell_rg53.92
Envelope Rg envelope_rg46.53
Shape Rg shape_rg47.46
Total Rg total_rg47.44
Total atoms total_atoms22813
Residues n_residues2888
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 dmax155.1
Rg (real space) rg_real47.54
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real1.4750e+09
I(0) uncertainty (real space) i0_real_error2.8860e+07
Rg (reciprocal space) rg_reciprocal47.73
I(0) (reciprocal space) i0_reciprocal1476000000.0000
Solution quality estimate total_estimate0.8782
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.4
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha272700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8h15A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id8h15B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id8h15C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain

8. Citations (1)

9. Files and Curves (10)