1nn8

CryoEM structure of poliovirus receptor bound to poliovirus

Method: ELECTRON MICROSCOPY Dmax: 166.2 Å Quality: REASONABLE

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 × 420 PDB declaration: 420-MERIC(420) Consistent with protein copy count Chain R; UniProt 28–329 Chain S; UniProt 28–329 Chain T; UniProt 28–329 Not recorded coat protein VP1 × 60 (P03300) coat protein VP2 × 60 (P03300) coat protein VP3 × 60 (P03300) coat protein VP4 × 60 (P03300) MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain R; UniProt 28–329 Chain S; UniProt 28–329 Chain T; UniProt 28–329 Not recorded coat protein VP1 × 1 (P03300) coat protein VP2 × 1 (P03300) coat protein VP3 × 1 (P03300) coat protein VP4 × 1 (P03300) MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain R; UniProt 28–329 Chain S; UniProt 28–329 Chain T; UniProt 28–329 Not recorded coat protein VP1 × 5 (P03300) coat protein VP2 × 5 (P03300) coat protein VP3 × 5 (P03300) coat protein VP4 × 5 (P03300) MYR MYRISTIC ACID × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain R; UniProt 28–329 Chain S; UniProt 28–329 Chain T; UniProt 28–329 Not recorded coat protein VP1 × 6 (P03300) coat protein VP2 × 6 (P03300) coat protein VP3 × 6 (P03300) coat protein VP4 × 6 (P03300) MYR MYRISTIC ACID × 6 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain R; UniProt 28–329 Chain S; UniProt 28–329 Chain T; UniProt 28–329 Not recorded coat protein VP1 × 1 (P03300) coat protein VP2 × 1 (P03300) coat protein VP3 × 1 (P03300) coat protein VP4 × 1 (P03300) MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 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 1–302; UniProt 28–329 Author chain S; PDBConstruct 1–302; UniProt 28–329 Author chain T; PDBConstruct 1–302; UniProt 28–329

coat protein VP1

Human poliovirus 1 Mahoney

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 × 420 PDB declaration: 420-MERIC(420) Consistent with protein copy count Chain 1; UniProt 579–880 Chain 2; UniProt 69–340 Chain 3; UniProt 341–575 Chain 4; UniProt 1–68 Not recorded poliovirus receptor × 180 (P15151) MYR MYRISTIC ACID × 60 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 579–880 Chain 2; UniProt 69–340 Chain 3; UniProt 341–575 Chain 4; UniProt 1–68 Not recorded poliovirus receptor × 3 (P15151) MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain 1; UniProt 579–880 Chain 2; UniProt 69–340 Chain 3; UniProt 341–575 Chain 4; UniProt 1–68 Not recorded poliovirus receptor × 15 (P15151) MYR MYRISTIC ACID × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain 1; UniProt 579–880 Chain 2; UniProt 69–340 Chain 3; UniProt 341–575 Chain 4; UniProt 1–68 Not recorded poliovirus receptor × 18 (P15151) MYR MYRISTIC ACID × 6 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain 1; UniProt 579–880 Chain 2; UniProt 69–340 Chain 3; UniProt 341–575 Chain 4; UniProt 1–68 Not recorded poliovirus receptor × 3 (P15151) MYR MYRISTIC ACID × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 15.00 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 2, 3, 4, 5
Chains and sequence ranges Author chain 1; PDBConstruct 1–302; UniProt 579–880 Author chain 2; PDBConstruct 1–272; UniProt 69–340 Author chain 3; PDBConstruct 1–235; UniProt 341–575 Author chain 4; PDBConstruct 1–68; UniProt 1–68

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 1nn8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nn8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nn8
Deposition date deposition_date2003-01-13
Structure title titleCryoEM structure of poliovirus receptor bound to poliovirus
Keywords keywordsicosahedral virus, picornavirus, Virus-Receptor COMPLEX; Virus/Receptor
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.91
Radius of gyration Rg (electron density) rg_electron50.36
Forward intensity I(0) i0536545000.00
Molecular weight molecular_weight192820.0 kDa
Excluded volume excluded_volume235340 ų
Envelope volume envelope_volume178070 ų
Hydration-shell volume shell_volume34063 ų
Envelope diameter envelope_diameter177.1
Shell Rg shell_rg44.00
Envelope Rg envelope_rg50.12
Shape Rg shape_rg50.53
Total Rg total_rg50.21
Total atoms total_atoms1
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 dmax166.2
Rg (real space) rg_real50.25
Rg uncertainty (real space) rg_real_error2.01
I(0) (real space) i0_real5.3650e+08
I(0) uncertainty (real space) i0_real_error1.0100e+07
Rg (reciprocal space) rg_reciprocal48.92
I(0) (reciprocal space) i0_reciprocal535600000.0000
Solution quality estimate total_estimate0.7238
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.660
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4414000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.652; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.393; Smooth: 0.057

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1nn81_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn82_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn83_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn84_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn8r_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn8s_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1nn8t_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes

8. Citations (1)

9. Files and Curves (10)