8yze

The JN.1 spike protein (S) in complex with ACE2.

Method: ELECTRON MICROSCOPY Dmax: 221.6 Å Quality: GOOD

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

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 14–1208 Chain B; UniProt 14–1208 Chain C; UniProt 14–1208 Not recorded Angiotensin-converting enzyme 2 × 3 (Q9BYF1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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 25–1211; UniProt 14–1208 Author chain B; PDBConstruct 25–1211; UniProt 14–1208 Author chain C; PDBConstruct 25–1211; UniProt 14–1208

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

UniProt P10104

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 458–481 Chain B; UniProt 458–481 Chain C; UniProt 458–481 Not recorded Angiotensin-converting enzyme 2 × 3 (Q9BYF1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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.

104 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1214–1237; UniProt 458–481 Author chain B; PDBConstruct 1214–1237; UniProt 458–481 Author chain C; PDBConstruct 1214–1237; UniProt 458–481

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–732 Chain H; UniProt 1–732 Chain I; UniProt 1–732 Not recorded Spike glycoprotein,Fibritin,Expression Tag × 3 (P0DTC2,P10104) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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 G; PDBConstruct 1–732; UniProt 1–732 Author chain H; PDBConstruct 1–732; UniProt 1–732 Author chain I; PDBConstruct 1–732; UniProt 1–732

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 8yze

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8yze
Deposition date deposition_date2024-04-06
Structure title titleThe JN.1 spike protein (S) in complex with ACE2.
Keywords keywordsACE2, Viral protein; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier73.85
Radius of gyration Rg (electron density) rg_electron73.89
Forward intensity I(0) i04153940000.00
Molecular weight molecular_weight552750.0 kDa
Excluded volume excluded_volume693400 ų
Envelope volume envelope_volume1182400 ų
Hydration-shell volume shell_volume140000 ų
Envelope diameter envelope_diameter262.5
Shell Rg shell_rg71.17
Envelope Rg envelope_rg69.97
Shape Rg shape_rg73.93
Total Rg total_rg73.70
Total atoms total_atoms38994
Residues n_residues4893
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 dmax221.6
Rg (real space) rg_real73.50
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real4.1410e+09
I(0) uncertainty (real space) i0_real_error7.6070e+07
Rg (reciprocal space) rg_reciprocal73.40
I(0) (reciprocal space) i0_reciprocal4149000000.0000
Solution quality estimate total_estimate0.8426
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary95.0
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0403
Highest regularization parameter α highest_alpha141400000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.051

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)