3epd

CryoEM structure of poliovirus receptor bound to poliovirus type 3

Method: ELECTRON MICROSCOPY Dmax: 141.8 Å Quality: GOOD

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

Poliovirus receptor

Homo sapiens

UniProt P15151

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 R; UniProt 30–242 Fragment:Poliovirus receptor CD155 D1D2 Mutation:N105D, N120S, N188Q, N218Q, N237S Poliovirus Type3 peptide × 60 protein VP1 × 60 (Q8B3S0) protein VP2 × 60 (Q8B3S0) protein VP4 × 60 (Q8B3S0) protein VP3 × 60 (Q8B3S0) SPH SPHINGOSINE × 60 MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 30–242 Fragment:Poliovirus receptor CD155 D1D2 Mutation:N105D, N120S, N188Q, N218Q, N237S Poliovirus Type3 peptide × 1 protein VP1 × 1 (Q8B3S0) protein VP2 × 1 (Q8B3S0) protein VP4 × 1 (Q8B3S0) protein VP3 × 1 (Q8B3S0) SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain R; UniProt 30–242 Fragment:Poliovirus receptor CD155 D1D2 Mutation:N105D, N120S, N188Q, N218Q, N237S Poliovirus Type3 peptide × 5 protein VP1 × 5 (Q8B3S0) protein VP2 × 5 (Q8B3S0) protein VP4 × 5 (Q8B3S0) protein VP3 × 5 (Q8B3S0) SPH SPHINGOSINE × 5 MYR MYRISTIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain R; UniProt 30–242 Fragment:Poliovirus receptor CD155 D1D2 Mutation:N105D, N120S, N188Q, N218Q, N237S Poliovirus Type3 peptide × 6 protein VP1 × 6 (Q8B3S0) protein VP2 × 6 (Q8B3S0) protein VP4 × 6 (Q8B3S0) protein VP3 × 6 (Q8B3S0) SPH SPHINGOSINE × 6 MYR MYRISTIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 30–242 Fragment:Poliovirus receptor CD155 D1D2 Mutation:N105D, N120S, N188Q, N218Q, N237S Poliovirus Type3 peptide × 1 protein VP1 × 1 (Q8B3S0) protein VP2 × 1 (Q8B3S0) protein VP4 × 1 (Q8B3S0) protein VP3 × 1 (Q8B3S0) SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

12 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PVR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–213; UniProt 30–242

protein VP1

Human poliovirus 3

UniProt Q8B3S0

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 600–878 Chain 2; UniProt 75–340 Chain 3; UniProt 341–575 Chain 4; UniProt 2–69 Not recorded Poliovirus receptor × 60 (P15151) Poliovirus Type3 peptide × 60 SPH SPHINGOSINE × 60 MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 600–878 Chain 2; UniProt 75–340 Chain 3; UniProt 341–575 Chain 4; UniProt 2–69 Not recorded Poliovirus receptor × 1 (P15151) Poliovirus Type3 peptide × 1 SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 600–878 Chain 2; UniProt 75–340 Chain 3; UniProt 341–575 Chain 4; UniProt 2–69 Not recorded Poliovirus receptor × 5 (P15151) Poliovirus Type3 peptide × 5 SPH SPHINGOSINE × 5 MYR MYRISTIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain 1; UniProt 600–878 Chain 2; UniProt 75–340 Chain 3; UniProt 341–575 Chain 4; UniProt 2–69 Not recorded Poliovirus receptor × 6 (P15151) Poliovirus Type3 peptide × 6 SPH SPHINGOSINE × 6 MYR MYRISTIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 600–878 Chain 2; UniProt 75–340 Chain 3; UniProt 341–575 Chain 4; UniProt 2–69 Not recorded Poliovirus receptor × 1 (P15151) Poliovirus Type3 peptide × 1 SPH SPHINGOSINE × 1 MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10mM Tris-HCl, 20mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q8B3S0_9ENTO
Isoform
PDB entities 3, 4, 5, 6
Chains and sequence ranges Author chain 1; PDBConstruct 1–279; UniProt 600–878 Author chain 2; PDBConstruct 1–266; UniProt 75–340 Author chain 4; PDBConstruct 1–68; UniProt 2–69 Author chain 3; PDBConstruct 1–235; UniProt 341–575

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 3epd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3epd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3epd
Deposition date deposition_date2008-09-29
Structure title titleCryoEM structure of poliovirus receptor bound to poliovirus type 3
Keywords keywords;CD155 structure Immunoglobulin Superfamily, poliovirus capsid jelly role, Cell adhesion, Cell membrane, Glycoprotein, Host-virus interaction, Immunoglobulin domain, Membrane, Receptor, Secreted, Transmembrane, VIRAL PROTEIN, VIRUS ;; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.22
Radius of gyration Rg (electron density) rg_electron36.21
Forward intensity I(0) i0213722000.00
Molecular weight molecular_weight117770.0 kDa
Excluded volume excluded_volume147400 ų
Envelope volume envelope_volume202730 ų
Hydration-shell volume shell_volume48304 ų
Envelope diameter envelope_diameter150.1
Shell Rg shell_rg40.41
Envelope Rg envelope_rg37.71
Shape Rg shape_rg36.17
Total Rg total_rg36.67
Total atoms total_atoms8290
Residues n_residues1058
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 dmax141.8
Rg (real space) rg_real36.48
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real2.1370e+08
I(0) uncertainty (real space) i0_real_error3.4450e+06
Rg (reciprocal space) rg_reciprocal36.31
I(0) (reciprocal space) i0_reciprocal213700000.0000
Solution quality estimate total_estimate0.7895
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.653
Kurtosis Kurtosis kurtosis0.441
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34120000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.512; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.748; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)