7xu4

Structure of SARS-CoV-2 D614G Spike Protein with Engineered x3 Disulfide (x3(D427C, V987C) and single Arg S1/S2 cleavage site), Locked-2 Conformation

Method: ELECTRON MICROSCOPY Dmax: 174.2 Å Quality: REASONABLE

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

Spike glycoprotein

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 Other combination Homooligomer Protein × 3 其他Polymer 12 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–1140 Chain B; UniProt 14–1140 Chain C; UniProt 14–1140 Mutation:D427C, D614G, V987C 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 39 BLA BILIVERDINE IX ALPHA × 3 EIC LINOLEIC ACID × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 5–1127; UniProt 14–1140 Author chain B; PDBConstruct 5–1127; UniProt 14–1140 Author chain C; PDBConstruct 5–1127; UniProt 14–1140

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 7xu4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xu4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7xu4
Deposition date deposition_date2022-05-18
Structure title titleStructure of SARS-CoV-2 D614G Spike Protein with Engineered x3 Disulfide (x3(D427C, V987C) and single Arg S1/S2 cleavage site), Locked-2 Conformation
Keywords keywordsprotein engineering, spike protein, SARS-CoV-2, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.56
Radius of gyration Rg (electron density) rg_electron49.03
Forward intensity I(0) i02070370000.00
Molecular weight molecular_weight384210.0 kDa
Excluded volume excluded_volume482130 ų
Envelope volume envelope_volume645160 ų
Hydration-shell volume shell_volume106490 ų
Envelope diameter envelope_diameter161.0
Shell Rg shell_rg54.99
Envelope Rg envelope_rg48.66
Shape Rg shape_rg49.07
Total Rg total_rg49.10
Total atoms total_atoms53367
Residues n_residues3330
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 dmax174.2
Rg (real space) rg_real49.41
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real2.0700e+09
I(0) uncertainty (real space) i0_real_error3.9610e+07
Rg (reciprocal space) rg_reciprocal49.56
I(0) (reciprocal space) i0_reciprocal2071000000.0000
Solution quality estimate total_estimate0.5795
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary168.7
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha352100000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 1.000; Sysdev: 0.087; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7xu4A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7xu4B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7xu4C01
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)