6acd

Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation

Method: ELECTRON MICROSCOPY Dmax: 163.4 Å Quality: GOOD

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

Spike glycoprotein

Human SARS 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 1–1196 Chain B; UniProt 1–1196 Chain C; UniProt 1–1196 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 5.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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_CVHSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1196; UniProt 1–1196 Author chain B; PDBConstruct 1–1196; UniProt 1–1196 Author chain C; PDBConstruct 1–1196; UniProt 1–1196

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 6acd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6acd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6acd
Deposition date deposition_date2018-07-26
Structure title titleTrypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation
Keywords keywordsSARS-CoV, spike, glycoprotein, Class I fusion protein, membrane fusion, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.29
Radius of gyration Rg (electron density) rg_electron49.97
Forward intensity I(0) i01748320000.00
Molecular weight molecular_weight352640.0 kDa
Excluded volume excluded_volume442430 ų
Envelope volume envelope_volume637520 ų
Hydration-shell volume shell_volume104620 ų
Envelope diameter envelope_diameter172.4
Shell Rg shell_rg55.17
Envelope Rg envelope_rg48.98
Shape Rg shape_rg50.02
Total Rg total_rg49.97
Total atoms total_atoms24845
Residues n_residues3187
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 dmax163.4
Rg (real space) rg_real50.16
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.7480e+09
I(0) uncertainty (real space) i0_real_error3.0540e+07
Rg (reciprocal space) rg_reciprocal50.39
I(0) (reciprocal space) i0_reciprocal1749000000.0000
Solution quality estimate total_estimate0.8891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha220500000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.875

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6acdA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id6acdB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id6acdC01
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)