9elf

Cryo-EM structure of SARS-CoV-2 Omicron KP.3.1.1 spike protein in complex with human ACE2

Method: ELECTRON MICROSCOPY Dmax: 210.9 Å Quality: GOOD

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

Processed angiotensin-converting enzyme 2

Homo sapiens

UniProt Q9BYF1

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 Heteromer Protein × 5 其他Polymer 16 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 19–615 Chain C; UniProt 19–615 Not recorded Spike glycoprotein × 3 (P0DTC2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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.

338 other PDB entries and 388 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–597; UniProt 19–615 Author chain C; PDBConstruct 1–597; UniProt 19–615

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 Heteromer Protein × 5 其他Polymer 16 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–1208 Chain F; UniProt 1–1208 Chain G; UniProt 1–1208 Not recorded Processed angiotensin-converting enzyme 2 × 2 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–1199; UniProt 1–1208 Author chain F; PDBConstruct 1–1199; UniProt 1–1208 Author chain G; PDBConstruct 1–1199; UniProt 1–1208

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 9elf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9elf
Deposition date deposition_date2024-12-04
Structure title titleCryo-EM structure of SARS-CoV-2 Omicron KP.3.1.1 spike protein in complex with human ACE2
Keywords keywordsSARS-CoV-2, COVID-19, Spike, hACE2, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.97
Radius of gyration Rg (electron density) rg_electron66.45
Forward intensity I(0) i03427960000.00
Molecular weight molecular_weight499860.0 kDa
Excluded volume excluded_volume627330 ų
Envelope volume envelope_volume961500 ų
Hydration-shell volume shell_volume126450 ų
Envelope diameter envelope_diameter245.5
Shell Rg shell_rg62.69
Envelope Rg envelope_rg64.59
Shape Rg shape_rg66.47
Total Rg total_rg66.29
Total atoms total_atoms35225
Residues n_residues4334
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 dmax210.9
Rg (real space) rg_real66.35
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real3.4250e+09
I(0) uncertainty (real space) i0_real_error7.3220e+07
Rg (reciprocal space) rg_reciprocal65.49
I(0) (reciprocal space) i0_reciprocal3422000000.0000
Solution quality estimate total_estimate0.8367
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.3
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.218
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0025
Highest regularization parameter α highest_alpha259700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.132

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)