30je

Herpes simplex virus 2 delta28-73 glycoprotein C ectodomain in complex with C3b

Method: ELECTRON MICROSCOPY Dmax: 129.1 Å Quality: GOOD

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

Envelope glycoprotein C

Human alphaherpesvirus 2

UniProt P03173

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–479 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 × 1 (P01024) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name GC_HHV2G
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–479; UniProt 1–479

Complement C3 beta chain

Homo sapiens

UniProt P01024

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 23–667 Chain C; UniProt 749–1663 Not recorded Envelope glycoprotein C × 1 (P03173) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

74 other PDB entries and 117 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO3_HUMAN
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–645; UniProt 23–667 Author chain C; PDBConstruct 1–915; UniProt 749–1663

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 30je

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 30je
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2. Structure Basics 2. Structure Basics

Entry ID entry_id30je
Deposition date deposition_date2026-04-29
Structure title titleHerpes simplex virus 2 delta28-73 glycoprotein C ectodomain in complex with C3b
Keywords keywordsProtein complex, complement protein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.08
Radius of gyration Rg (electron density) rg_electron37.76
Forward intensity I(0) i0182275000.00
Molecular weight molecular_weight111870.0 kDa
Excluded volume excluded_volume141460 ų
Envelope volume envelope_volume200940 ų
Hydration-shell volume shell_volume45374 ų
Envelope diameter envelope_diameter139.3
Shell Rg shell_rg42.41
Envelope Rg envelope_rg37.62
Shape Rg shape_rg37.77
Total Rg total_rg38.06
Total atoms total_atoms7888
Residues n_residues996
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 dmax129.1
Rg (real space) rg_real38.27
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real1.8230e+08
I(0) uncertainty (real space) i0_real_error3.1890e+06
Rg (reciprocal space) rg_reciprocal38.15
I(0) (reciprocal space) i0_reciprocal182300000.0000
Solution quality estimate total_estimate0.8722
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.0
Skewness Skewness skewness0.444
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25980000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)