9fa9

Coxsackievirus A9 bound with compound 16 (CL298)

Method: ELECTRON MICROSCOPY Dmax: 94.9 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 569–851 Chain B; UniProt 70–330 Chain C; UniProt 331–568 Chain D; UniProt 2–69 Not recorded A1IBS ~{N}-[(2-fluorophenyl)methyl]-4-[(4-methylpiperazin-1-yl)methyl]aniline × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;Sample was incubated for 15 s on the grid before blotted from the front for 1.5 s. Resolution 2.75 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 1–283; UniProt 569–851 Author chain B; PDBConstruct 1–261; UniProt 70–330 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 9fa9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fa9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fa9
Deposition date deposition_date2024-05-10
Structure title titleCoxsackievirus A9 bound with compound 16 (CL298)
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_guinier30.15
Radius of gyration Rg (electron density) rg_electron29.19
Forward intensity I(0) i0137853000.00
Molecular weight molecular_weight91842.0 kDa
Excluded volume excluded_volume114370 ų
Envelope volume envelope_volume147810 ų
Hydration-shell volume shell_volume41275 ų
Envelope diameter envelope_diameter101.1
Shell Rg shell_rg37.18
Envelope Rg envelope_rg29.78
Shape Rg shape_rg29.18
Total Rg total_rg29.96
Total atoms total_atoms12609
Residues n_residues821
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 dmax94.9
Rg (real space) rg_real30.08
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.3790e+08
I(0) uncertainty (real space) i0_real_error1.7970e+06
Rg (reciprocal space) rg_reciprocal30.11
I(0) (reciprocal space) i0_reciprocal137900000.0000
Solution quality estimate total_estimate0.6936
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.8
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27230000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 0.997; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)