9p3i

High-resolution in situ ANDV single tetramer structure

Method: ELECTRON MICROSCOPY Dmax: 170.1 Å Quality: GOOD

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 × 8 其他Polymer 16 PDB declaration: octameric(8) 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 Mutation:V535K Mutation:S1096L ;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 ; × 4 ;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 ; × 4 ;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 ; × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.35 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 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

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 9p3i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p3i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p3i
Deposition date deposition_date2025-06-13
Structure title titleHigh-resolution in situ ANDV single tetramer structure
Keywords keywordshantavirus, ANDV, viral glycoprotein, 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_guinier54.84
Radius of gyration Rg (electron density) rg_electron54.21
Forward intensity I(0) i02786460000.00
Molecular weight molecular_weight445630.0 kDa
Excluded volume excluded_volume558460 ų
Envelope volume envelope_volume841500 ų
Hydration-shell volume shell_volume124290 ų
Envelope diameter envelope_diameter171.8
Shell Rg shell_rg61.85
Envelope Rg envelope_rg52.42
Shape Rg shape_rg54.21
Total Rg total_rg54.42
Total atoms total_atoms31156
Residues n_residues3964
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 dmax170.1
Rg (real space) rg_real54.51
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real2.7860e+09
I(0) uncertainty (real space) i0_real_error5.3830e+07
Rg (reciprocal space) rg_reciprocal55.10
I(0) (reciprocal space) i0_reciprocal2789000000.0000
Solution quality estimate total_estimate0.8225
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.4
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha244600000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)