8jyo

Structure of SARS-CoV-2 XBB.1.5 spike glycoprotein in complex with ACE2 (2-up state)

Method: ELECTRON MICROSCOPY Dmax: 213.6 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 × 5 其他Polymer 13 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 28–1210 Chain B; UniProt 28–1210 Chain C; UniProt 28–1210 Mutation:F817P, A892P, A899P, A942P, K986P, V987P, R682G, R683S, R685G Processed angiotensin-converting enzyme 2 × 2 (Q9BYF1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;blotting time 5 s and blotting force 5. 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 24–1205; UniProt 28–1210 Author chain B; PDBConstruct 24–1205; UniProt 28–1210 Author chain C; PDBConstruct 24–1205; UniProt 28–1210

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 13 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 19–617 Chain E; UniProt 19–617 Not recorded Spike glycoprotein × 3 (P0DTC2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;blotting time 5 s and blotting force 5. 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.

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 1–599; UniProt 19–617 Author chain E; PDBConstruct 1–599; UniProt 19–617

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 8jyo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8jyo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8jyo
Deposition date deposition_date2023-07-03
Structure title titleStructure of SARS-CoV-2 XBB.1.5 spike glycoprotein in complex with ACE2 (2-up state)
Keywords keywordsspike protein, glycoprotein, VIRUS, VIRAL PROTEIN-PROTEIN BINDING complex; VIRAL PROTEIN/PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.89
Radius of gyration Rg (electron density) rg_electron69.00
Forward intensity I(0) i03242200000.00
Molecular weight molecular_weight485850.0 kDa
Excluded volume excluded_volume609510 ų
Envelope volume envelope_volume1004400 ų
Hydration-shell volume shell_volume128000 ų
Envelope diameter envelope_diameter234.9
Shell Rg shell_rg64.90
Envelope Rg envelope_rg65.82
Shape Rg shape_rg69.03
Total Rg total_rg68.82
Total atoms total_atoms34233
Residues n_residues4193
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 dmax213.6
Rg (real space) rg_real69.03
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real3.2420e+09
I(0) uncertainty (real space) i0_real_error6.9740e+07
Rg (reciprocal space) rg_reciprocal68.17
I(0) (reciprocal space) i0_reciprocal3237000000.0000
Solution quality estimate total_estimate0.8385
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary83.6
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha238600000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.045

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)