9zwe

Soluble ectodomain of Herpes simplex virus 2 (HSV-2) glycoprotein B (gB) in the prefusion conformation in complex with 2c and D48 Fabs

Method: ELECTRON MICROSCOPY Dmax: 175.2 Å Quality: GOOD

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

Envelope glycoprotein B

Human herpesvirus 2 strain HG52

UniProt P08666

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 74–731 Chain B; UniProt 74–731 Chain G; UniProt 74–731 Not recorded Antibody D48 Heavy Chain × 3 Antibody D48 Light Chain × 3 Antibody 2c Heavy Chain × 3 Antibody 2c Light Chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.75 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 GB_HHV2H
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–658; UniProt 74–731 Author chain B; PDBConstruct 1–658; UniProt 74–731 Author chain G; PDBConstruct 1–658; UniProt 74–731

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 9zwe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zwe
Deposition date deposition_date2026-01-01
Structure title titleSoluble ectodomain of Herpes simplex virus 2 (HSV-2) glycoprotein B (gB) in the prefusion conformation in complex with 2c and D48 Fabs
Keywords keywordsprefusion, ectodomain, viral fusion protein, 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_guinier53.91
Radius of gyration Rg (electron density) rg_electron54.05
Forward intensity I(0) i01765920000.00
Molecular weight molecular_weight348220.0 kDa
Excluded volume excluded_volume434340 ų
Envelope volume envelope_volume614380 ų
Hydration-shell volume shell_volume96051 ų
Envelope diameter envelope_diameter176.9
Shell Rg shell_rg54.93
Envelope Rg envelope_rg53.67
Shape Rg shape_rg54.01
Total Rg total_rg54.20
Total atoms total_atoms48423
Residues n_residues3024
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 dmax175.2
Rg (real space) rg_real53.77
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real1.7660e+09
I(0) uncertainty (real space) i0_real_error3.7020e+07
Rg (reciprocal space) rg_reciprocal54.02
I(0) (reciprocal space) i0_reciprocal1767000000.0000
Solution quality estimate total_estimate0.8743
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary72.5
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.455
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha90060000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.684

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)