29qj

Respiratory syncytial virus fusion protein N-terminal heptad repeat domain in complex with Double stapled peptide 4/4g

Method: X-RAY DIFFRACTION Dmax: 78.6 Å Quality: REASONABLE

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

Fusion glycoprotein F1

OrganismNot specified

UniProt P03420

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 159–209 Non-standard monomer:Yes (specific site not provided by mmCIF) Double stapled peptide 4/4g × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.32 Å R-free 0.232

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.

52 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FUS_HRSVA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–52; UniProt 159–209

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 29qj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 29qj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id29qj
Deposition date deposition_date2026-03-30
最后修订 last_revision2026-06-10
Structure title titleRespiratory syncytial virus fusion protein N-terminal heptad repeat domain in complex with Double stapled peptide 4/4g
Keywords keywords;Human Respiratory Syncytial Virus, Fusion Protein, Fusion Inhibitor, Stapled Peptide, Six Helix Bundle, Complex, ANTIVIRAL PROTEIN, 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_guinier19.16
Radius of gyration Rg (electron density) rg_electron19.55
Forward intensity I(0) i01006880.00
Molecular weight molecular_weight7428.0 kDa
Excluded volume excluded_volume9642 ų
Envelope volume envelope_volume12399 ų
Hydration-shell volume shell_volume7063 ų
Envelope diameter envelope_diameter74.5
Shell Rg shell_rg21.05
Envelope Rg envelope_rg20.52
Shape Rg shape_rg19.61
Total Rg total_rg19.72
Total atoms total_atoms1078
Residues n_residues62
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 dmax78.6
Rg (real space) rg_real19.83
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.0070e+06
I(0) uncertainty (real space) i0_real_error1.6090e+04
Rg (reciprocal space) rg_reciprocal19.73
I(0) (reciprocal space) i0_reciprocal1007000.0000
Solution quality estimate total_estimate0.6518
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.1
Skewness Skewness skewness0.750
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53040.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.159; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.004; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)