7xoa

SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with one mouse ACE2 Bound

Method: ELECTRON MICROSCOPY Dmax: 210.3 Å Quality: GOOD

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 1–1273 Chain B; UniProt 1–1273 Chain C; UniProt 1–1273 Mutation:R682G, R683S, R685S, F817P, A892P, A899P, A942P, K986P, V987P Angiotensin-converting enzyme 2 × 1 (Q8R0I0) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34 ZN ZINC ION × 1 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 1–1270; UniProt 1–1273 Author chain B; PDBConstruct 1–1270; UniProt 1–1273 Author chain C; PDBConstruct 1–1270; UniProt 1–1273

Angiotensin-converting enzyme 2

Mus musculus

UniProt Q8R0I0

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 D; UniProt 1–805 Not recorded Spike glycoprotein × 3 (P0DTC2) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 34 ZN ZINC ION × 1 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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–805; UniProt 1–805

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 7xoa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xoa
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7xoa
Deposition date deposition_date2022-05-01
Structure title titleSARS-CoV-2 Omicron BA.2 Variant Spike Trimer with one mouse ACE2 Bound
Keywords keywordsVIRAL 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_guinier61.03
Radius of gyration Rg (electron density) rg_electron61.55
Forward intensity I(0) i02372320000.00
Molecular weight molecular_weight414120.0 kDa
Excluded volume excluded_volume519930 ų
Envelope volume envelope_volume780450 ų
Hydration-shell volume shell_volume112440 ų
Envelope diameter envelope_diameter238.1
Shell Rg shell_rg58.08
Envelope Rg envelope_rg60.60
Shape Rg shape_rg61.58
Total Rg total_rg61.34
Total atoms total_atoms29202
Residues n_residues3670
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 dmax210.3
Rg (real space) rg_real61.64
Rg uncertainty (real space) rg_real_error2.06
I(0) (real space) i0_real2.3720e+09
I(0) uncertainty (real space) i0_real_error5.1700e+07
Rg (reciprocal space) rg_reciprocal60.48
I(0) (reciprocal space) i0_reciprocal2368000000.0000
Solution quality estimate total_estimate0.8217
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.6
Skewness Skewness skewness0.654
Kurtosis Kurtosis kurtosis0.121
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha370800000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.760; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.398

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7xoaA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7xoaB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7xoaC01
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)