7vxc

SARS-CoV-2 Kappa variant spike protein in C3 state

Method: ELECTRON MICROSCOPY Dmax: 212.1 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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1208 Chain B; UniProt 1–1208 Chain D; UniProt 1–1208 Not recorded Angiotensin-converting enzyme 2 × 1 (Q9BYF1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 1–1208; UniProt 1–1208 Author chain B; PDBConstruct 1–1208; UniProt 1–1208 Author chain D; PDBConstruct 1–1208; UniProt 1–1208

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 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 17–615 Not recorded Spike glycoprotein × 3 (P0DTC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 2
Chains and sequence ranges Author chain C; PDBConstruct 18–616; UniProt 17–615

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 7vxc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7vxc
Deposition date deposition_date2021-11-12
Structure title titleSARS-CoV-2 Kappa variant spike protein in C3 state
Keywords keywordsSARS-CoV-2, coronavirus, Kappa variant, B.1.617.1 lineage, spike protein, VIRAL PROTEIN, VIRAL PROTEIN-HYDROLASE complex; VIRAL PROTEIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.22
Radius of gyration Rg (electron density) rg_electron64.44
Forward intensity I(0) i02504920000.00
Molecular weight molecular_weight424560.0 kDa
Excluded volume excluded_volume532200 ų
Envelope volume envelope_volume839960 ų
Hydration-shell volume shell_volume114350 ų
Envelope diameter envelope_diameter235.1
Shell Rg shell_rg61.53
Envelope Rg envelope_rg62.04
Shape Rg shape_rg64.49
Total Rg total_rg64.17
Total atoms total_atoms46264
Residues n_residues3801
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 dmax212.1
Rg (real space) rg_real64.49
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real2.5040e+09
I(0) uncertainty (real space) i0_real_error4.5840e+07
Rg (reciprocal space) rg_reciprocal63.93
I(0) (reciprocal space) i0_reciprocal2502000000.0000
Solution quality estimate total_estimate0.6217
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary79.5
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.153
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0012
Highest regularization parameter α highest_alpha152500000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 1.000; Smooth: 0.330

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7vxcA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7vxcB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7vxcD01
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)