9yka

Cryo-EM structure of post-fusion EBV gB in complex with AMMO2 fab

Method: ELECTRON MICROSCOPY Dmax: 127.0 Å Quality: EXCELLENT

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

BALF4

human gammaherpesvirus 4

UniProt R4R670

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–688 Chain B; UniProt 1–688 Chain C; UniProt 1–688 Not recorded AMMO2 fab heavy chain × 3 AMMO2 fab light chain × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name R4R670_EBVG
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–688; UniProt 1–688 Author chain B; PDBConstruct 1–688; UniProt 1–688 Author chain C; PDBConstruct 1–688; UniProt 1–688

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 9yka

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yka
Deposition date deposition_date2025-10-06
Structure title titleCryo-EM structure of post-fusion EBV gB in complex with AMMO2 fab
Keywords keywordsPost-fusion, AMMO2, fab, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.96
Radius of gyration Rg (electron density) rg_electron39.44
Forward intensity I(0) i0393297000.00
Molecular weight molecular_weight158620.0 kDa
Excluded volume excluded_volume197210 ų
Envelope volume envelope_volume267210 ų
Hydration-shell volume shell_volume58028 ų
Envelope diameter envelope_diameter129.8
Shell Rg shell_rg43.98
Envelope Rg envelope_rg39.02
Shape Rg shape_rg39.46
Total Rg total_rg39.65
Total atoms total_atoms11157
Residues n_residues1380
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 dmax127.0
Rg (real space) rg_real39.79
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real3.9330e+08
I(0) uncertainty (real space) i0_real_error6.4510e+06
Rg (reciprocal space) rg_reciprocal39.90
I(0) (reciprocal space) i0_reciprocal393300000.0000
Solution quality estimate total_estimate0.9056
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.8
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.579
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25910000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)