9fo2

Coxsackievirus A9 bound with compound 15 (CL278)

Method: ELECTRON MICROSCOPY Dmax: 96.3 Å Quality: REASONABLE

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

Capsid protein VP1

OrganismNot specified

UniProt P21404

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 homooligomer Homooligomer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain A; UniProt 569–867 Chain B; UniProt 79–329 Chain C; UniProt 331–568 Chain D; UniProt 2–69 Not recorded A1IEI ~{N}-[(4-fluorophenyl)methyl]-4-[(4-methylpiperazin-1-yl)methyl]aniline × 60 MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;Sample was blotted from the front for 1.5 s. Resolution 2.58 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.

12 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_CXA9
Isoform
PDB entities 1, 2, 3, 4
Chains and sequence ranges Author chain A; PDBConstruct 1–299; UniProt 569–867 Author chain B; PDBConstruct 1–251; UniProt 79–329 Author chain C; PDBConstruct 1–238; UniProt 331–568 Author chain D; 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 9fo2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fo2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fo2
Deposition date deposition_date2024-06-11
Structure title titleCoxsackievirus A9 bound with compound 15 (CL278)
Keywords keywordsAntiviral, capsid stabilizer, hydrophobic pocket, cryoEM, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.17
Radius of gyration Rg (electron density) rg_electron29.26
Forward intensity I(0) i0138936000.00
Molecular weight molecular_weight92426.0 kDa
Excluded volume excluded_volume115190 ų
Envelope volume envelope_volume148980 ų
Hydration-shell volume shell_volume41440 ų
Envelope diameter envelope_diameter101.9
Shell Rg shell_rg37.27
Envelope Rg envelope_rg29.89
Shape Rg shape_rg29.24
Total Rg total_rg30.04
Total atoms total_atoms12738
Residues n_residues825
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 dmax96.3
Rg (real space) rg_real30.10
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.3890e+08
I(0) uncertainty (real space) i0_real_error2.0320e+06
Rg (reciprocal space) rg_reciprocal30.13
I(0) (reciprocal space) i0_reciprocal138900000.0000
Solution quality estimate total_estimate0.6734
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27560000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 0.050; Positv: 1.000; Valcen: 0.998; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)