8kek

Monomer state of SARS-CoV Spike protein complexed with antibody PW5-535

Method: ELECTRON MICROSCOPY Dmax: 116.2 Å Quality: EXCELLENT

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

Spike glycoprotein

Severe acute respiratory syndrome coronavirus 2

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1190 Mutation:K968P, V969P, S577A PW5-535 heavy chain × 1 PW5-535 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–1190; UniProt 1–1190

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 8kek

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8kek
Deposition date deposition_date2023-08-11
Structure title titleMonomer state of SARS-CoV Spike protein complexed with antibody PW5-535
Keywords keywordsAntibody, VIRAL PROTEIN, IMMUNE SYSTEM-VIRAL PROTEIN complex; IMMUNE SYSTEM/VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.89
Radius of gyration Rg (electron density) rg_electron36.52
Forward intensity I(0) i0183258000.00
Molecular weight molecular_weight109440.0 kDa
Excluded volume excluded_volume137130 ų
Envelope volume envelope_volume195430 ų
Hydration-shell volume shell_volume46327 ų
Envelope diameter envelope_diameter127.3
Shell Rg shell_rg41.17
Envelope Rg envelope_rg36.11
Shape Rg shape_rg36.50
Total Rg total_rg36.92
Total atoms total_atoms7721
Residues n_residues994
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 dmax116.2
Rg (real space) rg_real36.83
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.8330e+08
I(0) uncertainty (real space) i0_real_error3.2310e+06
Rg (reciprocal space) rg_reciprocal36.87
I(0) (reciprocal space) i0_reciprocal183300000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.2
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16240000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)