7rzs

Cryo-EM structure of the SARS-CoV-2 HR1HR2 fusion core complex with L938F mutation

Method: ELECTRON MICROSCOPY Dmax: 111.6 Å Quality: REASONABLE

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

;SARS-CoV-2 HR1 L938F linked to a scaffold,Spike protein S2' ;

Severe acute respiratory syndrome coronavirus 2

UniProt B2J981

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 5–178 Chain B; UniProt 5–178 Chain C; UniProt 5–178 Mutation:L938F ;Spike protein S2' ; × 3 (P0DTC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2J981_NOSP7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–184; UniProt 5–178 Author chain B; PDBConstruct 11–184; UniProt 5–178 Author chain C; PDBConstruct 11–184; UniProt 5–178

;SARS-CoV-2 HR1 L938F linked to a scaffold,Spike protein S2' ;

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 917–988 Chain B; UniProt 917–988 Chain C; UniProt 917–988 Chain D; UniProt 1162–1201 Chain E; UniProt 1162–1201 Chain F; UniProt 1162–1201 Mutation:L938F No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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, 2
Chains and sequence ranges Author chain A; PDBConstruct 186–257; UniProt 917–988 Author chain B; PDBConstruct 186–257; UniProt 917–988 Author chain C; PDBConstruct 186–257; UniProt 917–988 Author chain D; PDBConstruct 2–41; UniProt 1162–1201 Author chain E; PDBConstruct 2–41; UniProt 1162–1201 Author chain F; PDBConstruct 2–41; UniProt 1162–1201

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 7rzs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rzs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7rzs
Deposition date deposition_date2021-08-27
Structure title titleCryo-EM structure of the SARS-CoV-2 HR1HR2 fusion core complex with L938F mutation
Keywords keywordsspike, HR1HR2, fusion, L938F, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.97
Radius of gyration Rg (electron density) rg_electron29.59
Forward intensity I(0) i020893600.00
Molecular weight molecular_weight34773.0 kDa
Excluded volume excluded_volume43452 ų
Envelope volume envelope_volume53799 ų
Hydration-shell volume shell_volume18295 ų
Envelope diameter envelope_diameter107.9
Shell Rg shell_rg30.38
Envelope Rg envelope_rg30.70
Shape Rg shape_rg29.58
Total Rg total_rg29.71
Total atoms total_atoms2445
Residues n_residues324
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 dmax111.6
Rg (real space) rg_real29.61
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real2.0890e+07
I(0) uncertainty (real space) i0_real_error3.7050e+05
Rg (reciprocal space) rg_reciprocal29.33
I(0) (reciprocal space) i0_reciprocal20890000.0000
Solution quality estimate total_estimate0.6421
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.768
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20480000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.133; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.016; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)