9x3k

apo state of Mengla Virus Glycoprotein

Method: ELECTRON MICROSCOPY Dmax: 89.8 Å Quality: EXCELLENT

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

Envelope glycoprotein

Dianlovirus menglaense

UniProt A0A3S8UVK3

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 Homooligomer Protein × 3 其他Polymer 6 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–662 Chain B; UniProt 1–662 Chain C; UniProt 1–662 Not recorded ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.08 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 A0A3S8UVK3_9MONO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–662; UniProt 1–662 Author chain B; PDBConstruct 1–662; UniProt 1–662 Author chain C; PDBConstruct 1–662; UniProt 1–662

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 9x3k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x3k
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9x3k
Deposition date deposition_date2025-10-09
Structure title titleapo state of Mengla Virus Glycoprotein
Keywords keywordsMengla Virus Glycoprotein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.49
Radius of gyration Rg (electron density) rg_electron29.02
Forward intensity I(0) i0148688000.00
Molecular weight molecular_weight97930.0 kDa
Excluded volume excluded_volume123400 ų
Envelope volume envelope_volume159330 ų
Hydration-shell volume shell_volume43889 ų
Envelope diameter envelope_diameter89.4
Shell Rg shell_rg37.93
Envelope Rg envelope_rg28.93
Shape Rg shape_rg28.98
Total Rg total_rg30.04
Total atoms total_atoms6885
Residues n_residues822
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 dmax89.8
Rg (real space) rg_real30.26
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.4870e+08
I(0) uncertainty (real space) i0_real_error2.0400e+06
Rg (reciprocal space) rg_reciprocal30.36
I(0) (reciprocal space) i0_reciprocal148700000.0000
Solution quality estimate total_estimate0.9100
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.5
Skewness Skewness skewness0.010
Kurtosis Kurtosis kurtosis-0.677
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83920000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)