10or

Cryo-EM structure of Sudan Ebolavirus GP bound by three neutralizing antibodies 316L, 523S and 294S

Method: ELECTRON MICROSCOPY Dmax: 164.7 Å Quality: GOOD

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

Envelope glycoprotein 1

Sudan ebolavirus

UniProt R4QJ45

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 24 其他Polymer 3 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 32–235 Chain B; UniProt 510–631 Chain C; UniProt 32–235 Chain D; UniProt 510–631 Chain E; UniProt 32–235 Chain F; UniProt 510–631 Not recorded 316L Heavy Chain × 3 316L Light Chain × 3 523S Heavy Chain × 3 523S Light Chain × 3 294S Heavy Chain × 3 294S Light Chain × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.46 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name R4QJ45_9MONO
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–204; UniProt 32–235 Author chain C; PDBConstruct 1–204; UniProt 32–235 Author chain E; PDBConstruct 1–204; UniProt 32–235 Author chain B; PDBConstruct 1–122; UniProt 510–631 Author chain D; PDBConstruct 1–122; UniProt 510–631 Author chain F; PDBConstruct 1–122; UniProt 510–631

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 10or

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10or
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10or
Deposition date deposition_date2026-01-29
Structure title titleCryo-EM structure of Sudan Ebolavirus GP bound by three neutralizing antibodies 316L, 523S and 294S
Keywords keywordsSUDV, neutralizing mAbs, 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_guinier51.05
Radius of gyration Rg (electron density) rg_electron50.95
Forward intensity I(0) i01632320000.00
Molecular weight molecular_weight330000.0 kDa
Excluded volume excluded_volume409840 ų
Envelope volume envelope_volume586320 ų
Hydration-shell volume shell_volume95755 ų
Envelope diameter envelope_diameter166.6
Shell Rg shell_rg54.44
Envelope Rg envelope_rg49.87
Shape Rg shape_rg50.90
Total Rg total_rg51.20
Total atoms total_atoms23250
Residues n_residues2883
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 dmax164.7
Rg (real space) rg_real50.99
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real1.6320e+09
I(0) uncertainty (real space) i0_real_error3.0710e+07
Rg (reciprocal space) rg_reciprocal51.10
I(0) (reciprocal space) i0_reciprocal1633000000.0000
Solution quality estimate total_estimate0.8601
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.8
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.365
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87320000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.625

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)