1xyr

Poliovirus 135S cell entry intermediate

Method: ELECTRON MICROSCOPY Dmax: 92.3 Å Quality: GOOD

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

Genome polyprotein, Coat protein 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 homooligomer Homooligomer Protein × 420 PDB declaration: 420-MERIC(420) Consistent with protein copy count Chain 1; UniProt 649–880 Chain 2; UniProt 96–332 Chain 3; UniProt 390–571 Chain 5; UniProt 341–352 Chain 6; UniProt 354–389 Chain 7; UniProt 81–94 Chain 8; UniProt 620–630 Fragment:residues 649-880 Fragment:residues 96-332 Fragment:residues 390-571 Fragment:residues 341-352 Fragment:residues 354-389 Fragment:residues 81-94 Fragment:residues 620-630 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20mM HEPES, 2mM CaCl2;pH 7.4;20mM HEPES, 2mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge freezing into liquid ethane Resolution 11.00 Å
2 Protein homooligomer Homooligomer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 649–880 Chain 2; UniProt 96–332 Chain 3; UniProt 390–571 Chain 5; UniProt 341–352 Chain 6; UniProt 354–389 Chain 7; UniProt 81–94 Chain 8; UniProt 620–630 Fragment:residues 649-880 Fragment:residues 96-332 Fragment:residues 390-571 Fragment:residues 341-352 Fragment:residues 354-389 Fragment:residues 81-94 Fragment:residues 620-630 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20mM HEPES, 2mM CaCl2;pH 7.4;20mM HEPES, 2mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge freezing into liquid ethane Resolution 11.00 Å
3 Protein homooligomer Homooligomer Protein × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain 1; UniProt 649–880 Chain 2; UniProt 96–332 Chain 3; UniProt 390–571 Chain 5; UniProt 341–352 Chain 6; UniProt 354–389 Chain 7; UniProt 81–94 Chain 8; UniProt 620–630 Fragment:residues 649-880 Fragment:residues 96-332 Fragment:residues 390-571 Fragment:residues 341-352 Fragment:residues 354-389 Fragment:residues 81-94 Fragment:residues 620-630 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20mM HEPES, 2mM CaCl2;pH 7.4;20mM HEPES, 2mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge freezing into liquid ethane Resolution 11.00 Å
4 Protein homooligomer Homooligomer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain 1; UniProt 649–880 Chain 2; UniProt 96–332 Chain 3; UniProt 390–571 Chain 5; UniProt 341–352 Chain 6; UniProt 354–389 Chain 7; UniProt 81–94 Chain 8; UniProt 620–630 Fragment:residues 649-880 Fragment:residues 96-332 Fragment:residues 390-571 Fragment:residues 341-352 Fragment:residues 354-389 Fragment:residues 81-94 Fragment:residues 620-630 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20mM HEPES, 2mM CaCl2;pH 7.4;20mM HEPES, 2mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge freezing into liquid ethane Resolution 11.00 Å
5 Protein homooligomer Homooligomer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 649–880 Chain 2; UniProt 96–332 Chain 3; UniProt 390–571 Chain 5; UniProt 341–352 Chain 6; UniProt 354–389 Chain 7; UniProt 81–94 Chain 8; UniProt 620–630 Fragment:residues 649-880 Fragment:residues 96-332 Fragment:residues 390-571 Fragment:residues 341-352 Fragment:residues 354-389 Fragment:residues 81-94 Fragment:residues 620-630 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20mM HEPES, 2mM CaCl2;pH 7.4;20mM HEPES, 2mM CaCl2 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge freezing into liquid ethane Resolution 11.00 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 POLH_POL1M
Isoform
PDB entities 1, 2, 3, 4, 5, 6, 7
Chains and sequence ranges Author chain 1; PDBConstruct 1–232; UniProt 649–880 Author chain 2; PDBConstruct 1–237; UniProt 96–332 Author chain 3; PDBConstruct 1–182; UniProt 390–571 Author chain 5; PDBConstruct 1–12; UniProt 341–352 Author chain 6; PDBConstruct 1–36; UniProt 354–389 Author chain 7; PDBConstruct 1–14; UniProt 81–94 Author chain 8; PDBConstruct 1–11; UniProt 620–630

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 1xyr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1xyr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1xyr
Deposition date deposition_date2004-11-10
Structure title titlePoliovirus 135S cell entry intermediate
Keywords keywordsBETA BARREL, VIRAL CAPSID, CELL ENTRY INTERMEDIATE, Icosahedral virus, Virus; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.31
Radius of gyration Rg (electron density) rg_electron28.70
Forward intensity I(0) i099447100.00
Molecular weight molecular_weight80477.0 kDa
Excluded volume excluded_volume98191 ų
Envelope volume envelope_volume83883 ų
Hydration-shell volume shell_volume26867 ų
Envelope diameter envelope_diameter99.7
Shell Rg shell_rg32.65
Envelope Rg envelope_rg27.65
Shape Rg shape_rg28.81
Total Rg total_rg28.99
Total atoms total_atoms
Residues n_residues
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 dmax92.3
Rg (real space) rg_real29.32
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real9.9450e+07
I(0) uncertainty (real space) i0_real_error1.4240e+06
Rg (reciprocal space) rg_reciprocal29.32
I(0) (reciprocal space) i0_reciprocal99450000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.381
Kurtosis Kurtosis kurtosis-0.262
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16980000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.858

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1xyr11
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

8. Citations (1)

9. Files and Curves (10)