9oco

SIPV3-2E1 Complex

Method: ELECTRON MICROSCOPY Dmax: 110.7 Å Quality: GOOD

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

VP1

OrganismNot specified

UniProt P03302

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 × 360 PDB declaration: 360-meric(360) Consistent with protein copy count Chain 1; UniProt 579–878 Chain 2; UniProt 70–340 Chain 3; UniProt 341–578 Chain 4; UniProt 2–69 Not recorded 2E1 Heavy Chain × 60 2E1 Light Chain × 60 PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 579–878 Chain 2; UniProt 70–340 Chain 3; UniProt 341–578 Chain 4; UniProt 2–69 Not recorded 2E1 Heavy Chain × 1 2E1 Light Chain × 1 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 579–878 Chain 2; UniProt 70–340 Chain 3; UniProt 341–578 Chain 4; UniProt 2–69 Not recorded 2E1 Heavy Chain × 5 2E1 Light Chain × 5 PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain 1; UniProt 579–878 Chain 2; UniProt 70–340 Chain 3; UniProt 341–578 Chain 4; UniProt 2–69 Not recorded 2E1 Heavy Chain × 6 2E1 Light Chain × 6 PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 579–878 Chain 2; UniProt 70–340 Chain 3; UniProt 341–578 Chain 4; UniProt 2–69 Not recorded 2E1 Heavy Chain × 1 2E1 Light Chain × 1 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

11 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL3L
Isoform
PDB entities 1, 2, 3, 4
Chains and sequence ranges Author chain 1; PDBConstruct 1–300; UniProt 579–878 Author chain 2; PDBConstruct 1–271; UniProt 70–340 Author chain 3; PDBConstruct 1–238; UniProt 341–578 Author chain 4; PDBConstruct 1–68; UniProt 2–69

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 9oco

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oco
Deposition date deposition_date2025-04-24
Structure title titleSIPV3-2E1 Complex
Keywords keywordsVirus, Antibody, Complex; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.32
Radius of gyration Rg (electron density) rg_electron33.61
Forward intensity I(0) i0221504000.00
Molecular weight molecular_weight118810.0 kDa
Excluded volume excluded_volume148230 ų
Envelope volume envelope_volume195790 ų
Hydration-shell volume shell_volume48057 ų
Envelope diameter envelope_diameter113.1
Shell Rg shell_rg40.71
Envelope Rg envelope_rg33.76
Shape Rg shape_rg33.58
Total Rg total_rg34.25
Total atoms total_atoms16480
Residues n_residues1071
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 dmax110.7
Rg (real space) rg_real34.28
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.2150e+08
I(0) uncertainty (real space) i0_real_error3.5650e+06
Rg (reciprocal space) rg_reciprocal34.31
I(0) (reciprocal space) i0_reciprocal221500000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha43970000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)