9wdp

Cyro-EM structure of prefusion RSV fusion glycoprotein in complex with Ziresovir and motavizumab Fab

Method: ELECTRON MICROSCOPY Dmax: 105.1 Å Quality: GOOD

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

Fusion glycoprotein F0,Fibritin

Tequatrovirus T4

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 Insufficient information Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–513 Chain B; UniProt 1–513 Chain C; UniProt 1–513 Not recorded Motavizumab Fab heavy chain × 3 Motavizumab Fab light chain × 3 A1EV1 ~{N}-[(3-azanyloxetan-3-yl)methyl]-2-[1,1-bis(oxidanylidene)-3,5-dihydro-2~{H}-1$l^{6},4-benzothiazepin-4-yl]-6-methyl-quinazolin-4-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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.

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 1–513; UniProt 1–513 Author chain B; PDBConstruct 1–513; UniProt 1–513 Author chain C; PDBConstruct 1–513; UniProt 1–513

Fusion glycoprotein F0,Fibritin

Tequatrovirus T4

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 458–485 Chain B; UniProt 458–485 Chain C; UniProt 458–485 Not recorded Motavizumab Fab heavy chain × 3 Motavizumab Fab light chain × 3 A1EV1 ~{N}-[(3-azanyloxetan-3-yl)methyl]-2-[1,1-bis(oxidanylidene)-3,5-dihydro-2~{H}-1$l^{6},4-benzothiazepin-4-yl]-6-methyl-quinazolin-4-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 516–543; UniProt 458–485 Author chain B; PDBConstruct 516–543; UniProt 458–485 Author chain C; PDBConstruct 516–543; UniProt 458–485

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 9wdp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wdp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9wdp
Deposition date deposition_date2025-08-19
Structure title titleCyro-EM structure of prefusion RSV fusion glycoprotein in complex with Ziresovir and motavizumab Fab
Keywords keywordsInhibitor, Complex, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.72
Radius of gyration Rg (electron density) rg_electron33.12
Forward intensity I(0) i0762846000.00
Molecular weight molecular_weight150040.0 kDa
Excluded volume excluded_volume145680 ų
Envelope volume envelope_volume262560 ų
Hydration-shell volume shell_volume62046 ų
Envelope diameter envelope_diameter114.2
Shell Rg shell_rg42.46
Envelope Rg envelope_rg33.43
Shape Rg shape_rg33.17
Total Rg total_rg33.55
Total atoms total_atoms11338
Residues n_residues1454
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 dmax105.1
Rg (real space) rg_real33.52
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real7.6280e+08
I(0) uncertainty (real space) i0_real_error1.2080e+07
Rg (reciprocal space) rg_reciprocal33.64
I(0) (reciprocal space) i0_reciprocal762900000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha122300000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)