8i9b

S-ECD (Omicron BA.2.75) in complex with PD of ACE2

Method: ELECTRON MICROSCOPY Dmax: 211.6 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 Other combination Heteromer Protein × 6 其他Polymer 37 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1206 Chain B; UniProt 1–1206 Chain C; UniProt 1–1206 Mutation:R682G, R683S, R685S, F817P, A892P, A899P, A942P, K986P, V987P Processed angiotensin-converting enzyme 2 × 3 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 37 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 29 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 1–1204; UniProt 1–1206 Author chain B; PDBConstruct 1–1204; UniProt 1–1206 Author chain C; PDBConstruct 1–1204; UniProt 1–1206

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 × 6 其他Polymer 37 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 19–615 Chain E; UniProt 19–615 Chain F; 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 × 37 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 29 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 D; PDBConstruct 20–616; UniProt 19–615 Author chain E; PDBConstruct 20–616; UniProt 19–615 Author chain F; PDBConstruct 20–616; UniProt 19–615

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 8i9b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i9b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i9b
Deposition date deposition_date2023-02-06
Structure title titleS-ECD (Omicron BA.2.75) in complex with PD of ACE2
Keywords keywordsSARS-Cov-2, 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_guinier72.25
Radius of gyration Rg (electron density) rg_electron72.14
Forward intensity I(0) i04299250000.00
Molecular weight molecular_weight561180.0 kDa
Excluded volume excluded_volume703580 ų
Envelope volume envelope_volume1181000 ų
Hydration-shell volume shell_volume141080 ų
Envelope diameter envelope_diameter243.1
Shell Rg shell_rg71.60
Envelope Rg envelope_rg67.81
Shape Rg shape_rg72.16
Total Rg total_rg72.07
Total atoms total_atoms39539
Residues n_residues4786
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 dmax211.6
Rg (real space) rg_real72.07
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real4.2910e+09
I(0) uncertainty (real space) i0_real_error8.2940e+07
Rg (reciprocal space) rg_reciprocal71.99
I(0) (reciprocal space) i0_reciprocal4296000000.0000
Solution quality estimate total_estimate0.8436
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary86.6
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0297
Highest regularization parameter α highest_alpha186300000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.026

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)