9b4x

SARS CoV-2 full-length spike protein with Lys1269Ala and His1271Ala substitutions in the coatomer binding motif, 1RBD-up conformation (SPIKE-AXA)

Method: ELECTRON MICROSCOPY Dmax: 177.3 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 33 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1273 Chain B; UniProt 1–1273 Chain C; UniProt 1–1273 Mutation:;D614G variant, residues 682-685 RRAR substituted with GSAS, K986P, V987P, K1269A, H1271A, strep-tag inserted between residues 18 and 19 ; 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ;alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-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 × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.33 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 1–1312; UniProt 1–1273 Author chain B; PDBConstruct 1–1312; UniProt 1–1273 Author chain C; PDBConstruct 1–1312; UniProt 1–1273

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 9b4x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b4x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b4x
Deposition date deposition_date2024-03-21
Structure title titleSARS CoV-2 full-length spike protein with Lys1269Ala and His1271Ala substitutions in the coatomer binding motif, 1RBD-up conformation (SPIKE-AXA)
Keywords keywordsSARS CoV-2 full-length spike with Lys1269Ala and His1271Ala substitutions in the coatomer binding motif, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.99
Radius of gyration Rg (electron density) rg_electron52.64
Forward intensity I(0) i01940950000.00
Molecular weight molecular_weight372040.0 kDa
Excluded volume excluded_volume466840 ų
Envelope volume envelope_volume716700 ų
Hydration-shell volume shell_volume111810 ų
Envelope diameter envelope_diameter187.6
Shell Rg shell_rg57.30
Envelope Rg envelope_rg51.76
Shape Rg shape_rg52.68
Total Rg total_rg52.66
Total atoms total_atoms50511
Residues n_residues3159
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 dmax177.3
Rg (real space) rg_real52.88
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real1.9410e+09
I(0) uncertainty (real space) i0_real_error3.4590e+07
Rg (reciprocal space) rg_reciprocal53.06
I(0) (reciprocal space) i0_reciprocal1941000000.0000
Solution quality estimate total_estimate0.6458
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.1
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha352300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 0.007; Positv: 1.000; Valcen: 0.973; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)