9ma7

Cryo-EM structure of EBV gp350 D123 in complex with neutralizing antibody 1A12 and 1H5 and non-neutralizing antibody 2E9

Method: ELECTRON MICROSCOPY Dmax: 132.9 Å Quality: GOOD

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

Envelope glycoprotein GP350

human gammaherpesvirus 4

UniProt P03200

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–470 Not recorded 1H5 heavy chain no-CH2CH3 × 1 1H5 light chain × 1 1A12 heavy chain no-CH2CH3 × 1 1A12 light chain × 1 2E9 heavy chain no-CH2CH3 × 1 2E9 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.14 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP350_EBVB9
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–470; UniProt 1–470

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 9ma7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ma7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ma7
Deposition date deposition_date2025-03-14
Structure title titleCryo-EM structure of EBV gp350 D123 in complex with neutralizing antibody 1A12 and 1H5 and non-neutralizing antibody 2E9
Keywords keywords;Envelope glycoprotein GP350, Membrane antigen (MA), neutralizing antibody, 1A22, 1E5, 2E9, 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_guinier40.24
Radius of gyration Rg (electron density) rg_electron40.11
Forward intensity I(0) i0225051000.00
Molecular weight molecular_weight119750.0 kDa
Excluded volume excluded_volume148770 ų
Envelope volume envelope_volume206030 ų
Hydration-shell volume shell_volume44957 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg43.44
Envelope Rg envelope_rg39.42
Shape Rg shape_rg40.08
Total Rg total_rg40.40
Total atoms total_atoms8435
Residues n_residues1111
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 dmax132.9
Rg (real space) rg_real40.27
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real2.2510e+08
I(0) uncertainty (real space) i0_real_error4.0270e+06
Rg (reciprocal space) rg_reciprocal40.24
I(0) (reciprocal space) i0_reciprocal225000000.0000
Solution quality estimate total_estimate0.8893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.9
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.707
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20260000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)