8xz8

BA.2.86 Spike in complex with bovine ACE2 (bound 1 ACE2)

Method: ELECTRON MICROSCOPY Dmax: 207.4 Å Quality: GOOD

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

Angiotensin-converting enzyme

Bos taurus

UniProt Q2HJI5

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 × 4 其他Polymer 17 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–804 Not recorded Spike glycoprotein × 3 (P0DTC2) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ZN ZINC ION × 1 CL CHLORIDE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 36 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2HJI5_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–804; UniProt 1–804

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 × 4 其他Polymer 17 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–1208 Chain C; UniProt 1–1208 Chain D; UniProt 1–1208 Not recorded Angiotensin-converting enzyme × 1 (Q2HJI5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ZN ZINC ION × 1 CL CHLORIDE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 36 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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 B; PDBConstruct 3–1206; UniProt 1–1208 Author chain C; PDBConstruct 3–1206; UniProt 1–1208 Author chain D; PDBConstruct 3–1206; 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 8xz8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xz8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8xz8
Deposition date deposition_date2024-01-21
Structure title titleBA.2.86 Spike in complex with bovine ACE2 (bound 1 ACE2)
Keywords keywordsSARS-CoV-2, complex, Spike, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.17
Radius of gyration Rg (electron density) rg_electron60.65
Forward intensity I(0) i02647080000.00
Molecular weight molecular_weight436980.0 kDa
Excluded volume excluded_volume548290 ų
Envelope volume envelope_volume794930 ų
Hydration-shell volume shell_volume114600 ų
Envelope diameter envelope_diameter231.6
Shell Rg shell_rg58.33
Envelope Rg envelope_rg60.27
Shape Rg shape_rg60.67
Total Rg total_rg60.50
Total atoms total_atoms30785
Residues n_residues3785
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 dmax207.4
Rg (real space) rg_real60.77
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real2.6470e+09
I(0) uncertainty (real space) i0_real_error5.0800e+07
Rg (reciprocal space) rg_reciprocal59.65
I(0) (reciprocal space) i0_reciprocal2642000000.0000
Solution quality estimate total_estimate0.8177
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.8
Skewness Skewness skewness0.655
Kurtosis Kurtosis kurtosis0.076
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha381500000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.390

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)