9p3x

Structure of the ANDV dimer of tetramer at conformation I

Method: ELECTRON MICROSCOPY Dmax: 229.1 Å Quality: REASONABLE

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

Glycoprotein N

Orthohantavirus andesense

UniProt Q9E006

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 × 16 其他Polymer 32 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–651 Chain B; UniProt 652–1138 Chain C; UniProt 1–651 Chain D; UniProt 652–1138 Chain E; UniProt 1–651 Chain F; UniProt 652–1138 Chain G; UniProt 1–651 Chain H; UniProt 652–1138 Chain I; UniProt 1–651 Chain J; UniProt 652–1138 Chain K; UniProt 1–651 Chain L; UniProt 652–1138 Chain M; UniProt 1–651 Chain N; UniProt 652–1138 Chain O; UniProt 1–651 Chain P; UniProt 652–1138 Not recorded ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 8 ;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 ; × 8 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 8 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP_ANDV
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–651; UniProt 1–651 Author chain C; PDBConstruct 1–651; UniProt 1–651 Author chain E; PDBConstruct 1–651; UniProt 1–651 Author chain G; PDBConstruct 1–651; UniProt 1–651 Author chain I; PDBConstruct 1–651; UniProt 1–651 Author chain K; PDBConstruct 1–651; UniProt 1–651 Author chain M; PDBConstruct 1–651; UniProt 1–651 Author chain O; PDBConstruct 1–651; UniProt 1–651 Author chain B; PDBConstruct 1–487; UniProt 652–1138 Author chain D; PDBConstruct 1–487; UniProt 652–1138 Author chain F; PDBConstruct 1–487; UniProt 652–1138 Author chain H; PDBConstruct 1–487; UniProt 652–1138 Author chain J; PDBConstruct 1–487; UniProt 652–1138 Author chain L; PDBConstruct 1–487; UniProt 652–1138 Author chain N; PDBConstruct 1–487; UniProt 652–1138 Author chain P; PDBConstruct 1–487; UniProt 652–1138

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 9p3x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p3x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p3x
Deposition date deposition_date2025-06-14
Structure title titleStructure of the ANDV dimer of tetramer at conformation I
Keywords keywordshantavirus, ANDV, Gn-Gc, dimer of tetramer, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier84.02
Radius of gyration Rg (electron density) rg_electron84.33
Forward intensity I(0) i010859200000.00
Molecular weight molecular_weight891260.0 kDa
Excluded volume excluded_volume1116900 ų
Envelope volume envelope_volume1908000 ų
Hydration-shell volume shell_volume192560 ų
Envelope diameter envelope_diameter292.5
Shell Rg shell_rg78.66
Envelope Rg envelope_rg80.80
Shape Rg shape_rg84.34
Total Rg total_rg84.26
Total atoms total_atoms62312
Residues n_residues7928
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 dmax229.1
Rg (real space) rg_real80.84
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.0500e+10
I(0) uncertainty (real space) i0_real_error2.1120e+08
Rg (reciprocal space) rg_reciprocal82.06
I(0) (reciprocal space) i0_reciprocal10800000000.0000
Solution quality estimate total_estimate0.6730
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary84.4
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.3528
Highest regularization parameter α highest_alpha935700000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 0.982; Sysdev: 0.008; Positv: 1.000; Valcen: 0.991; Smooth: 0.030

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)