6psz

Poliovirus (Type 1 Mahoney), heat-catalysed 135S particle

Method: ELECTRON MICROSCOPY Dmax: 98.2 Å Quality: GOOD

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

VP1

OrganismNot specified

UniProt P03300

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 VP3 × 60 (Q8QYM4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 VP3 × 1 (Q8QYM4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 VP3 × 5 (Q8QYM4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 VP3 × 6 (Q8QYM4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 VP3 × 1 (Q8QYM4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

80 other PDB entries and 246 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–302; UniProt 580–881 Author chain 2; PDBConstruct 1–272; UniProt 70–341

VP3

OrganismNot specified

UniProt Q8QYM4

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain 3; UniProt 342–579 Fragment:UNP residues 342-579 VP1 × 60 (P03300) VP2 × 60 (P03300) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 3; UniProt 342–579 Fragment:UNP residues 342-579 VP1 × 1 (P03300) VP2 × 1 (P03300) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain 3; UniProt 342–579 Fragment:UNP residues 342-579 VP1 × 5 (P03300) VP2 × 5 (P03300) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain 3; UniProt 342–579 Fragment:UNP residues 342-579 VP1 × 6 (P03300) VP2 × 6 (P03300) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 3; UniProt 342–579 Fragment:UNP residues 342-579 VP1 × 1 (P03300) VP2 × 1 (P03300) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Tris-HCl, pH 7.5 + 2 mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

2 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8QYM4_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–238; UniProt 342–579

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 6psz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6psz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6psz
Deposition date deposition_date2019-07-14
Structure title titlePoliovirus (Type 1 Mahoney), heat-catalysed 135S particle
Keywords keywordspoliovirus, cell-entry intermediate, expanded virus, a-particle, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.66
Radius of gyration Rg (electron density) rg_electron28.91
Forward intensity I(0) i081858400.00
Molecular weight molecular_weight72382.0 kDa
Excluded volume excluded_volume90910 ų
Envelope volume envelope_volume111820 ų
Hydration-shell volume shell_volume32951 ų
Envelope diameter envelope_diameter103.5
Shell Rg shell_rg35.27
Envelope Rg envelope_rg29.55
Shape Rg shape_rg28.89
Total Rg total_rg29.56
Total atoms total_atoms10098
Residues n_residues646
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 dmax98.2
Rg (real space) rg_real29.73
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real8.1860e+07
I(0) uncertainty (real space) i0_real_error1.1770e+06
Rg (reciprocal space) rg_reciprocal29.71
I(0) (reciprocal space) i0_reciprocal81860000.0000
Solution quality estimate total_estimate0.8841
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha16770000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6psz100
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id6psz200
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id6psz300
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)