8zq7

Crystal structure of prefusion RSV F protein

Method: X-RAY DIFFRACTION Dmax: 146.3 Å Quality: GOOD

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

Fusion glycoprotein F0,Fibritin

Enterobacteria phage T6

UniProt A0A346FJN8

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 Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 458–484 Chain C; UniProt 458–484 Chain F; UniProt 458–484 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;8% Tacsimate pH6.0+20% PEG 3350 Resolution 2.77 Å R-free 0.242
2 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 458–484 Chain D; UniProt 458–484 Chain E; UniProt 458–484 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;8% Tacsimate pH6.0+20% PEG 3350 Resolution 2.77 Å R-free 0.242

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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A346FJN8_BPT6
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 488–514; UniProt 458–484 Author chain B; PDBConstruct 488–514; UniProt 458–484 Author chain C; PDBConstruct 488–514; UniProt 458–484 Author chain D; PDBConstruct 488–514; UniProt 458–484 Author chain E; PDBConstruct 488–514; UniProt 458–484 Author chain F; PDBConstruct 488–514; UniProt 458–484

Fusion glycoprotein F0,Fibritin

Enterobacteria phage T6

UniProt P12568

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 Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–99 Chain A; UniProt 136–513 Chain C; UniProt 26–99 Chain C; UniProt 136–513 Chain F; UniProt 26–99 Chain F; UniProt 136–513 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;8% Tacsimate pH6.0+20% PEG 3350 Resolution 2.77 Å R-free 0.242
2 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 26–99 Chain B; UniProt 136–513 Chain D; UniProt 26–99 Chain D; UniProt 136–513 Chain E; UniProt 26–99 Chain E; UniProt 136–513 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;8% Tacsimate pH6.0+20% PEG 3350 Resolution 2.77 Å R-free 0.242

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FUS_HRSV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–90; UniProt 26–99 Author chain A; PDBConstruct 106–483; UniProt 136–513 Author chain B; PDBConstruct 17–90; UniProt 26–99 Author chain B; PDBConstruct 106–483; UniProt 136–513 Author chain C; PDBConstruct 17–90; UniProt 26–99 Author chain C; PDBConstruct 106–483; UniProt 136–513 Author chain D; PDBConstruct 17–90; UniProt 26–99 Author chain D; PDBConstruct 106–483; UniProt 136–513 Author chain E; PDBConstruct 17–90; UniProt 26–99 Author chain E; PDBConstruct 106–483; UniProt 136–513 Author chain F; PDBConstruct 17–90; UniProt 26–99 Author chain F; PDBConstruct 106–483; UniProt 136–513

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 8zq7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zq7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zq7
Deposition date deposition_date2024-06-01
Structure title titleCrystal structure of prefusion RSV F protein
Keywords keywordsRSV, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.18
Radius of gyration Rg (electron density) rg_electron47.05
Forward intensity I(0) i01270470000.00
Molecular weight molecular_weight301080.0 kDa
Excluded volume excluded_volume379110 ų
Envelope volume envelope_volume510930 ų
Hydration-shell volume shell_volume88025 ų
Envelope diameter envelope_diameter151.4
Shell Rg shell_rg53.13
Envelope Rg envelope_rg46.39
Shape Rg shape_rg47.03
Total Rg total_rg47.35
Total atoms total_atoms21095
Residues n_residues2742
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 dmax146.3
Rg (real space) rg_real47.12
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real1.2700e+09
I(0) uncertainty (real space) i0_real_error2.1950e+07
Rg (reciprocal space) rg_reciprocal47.18
I(0) (reciprocal space) i0_reciprocal1271000000.0000
Solution quality estimate total_estimate0.8655
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.637
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha376600000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.437

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)