1pov

ROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 95.8 Å Quality: GOOD

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

POLIOVIRUS NATIVE EMPTY CAPSID (TYPE 1)

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 × 180 PDB declaration: 180-MERIC(180) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 60 SPH SPHINGOSINE × 60 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 1 SPH SPHINGOSINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å
3 Protein homooligomer Homooligomer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 5 SPH SPHINGOSINE × 5 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å
4 Protein homooligomer Homooligomer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 6 SPH SPHINGOSINE × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å
5 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 1 SPH SPHINGOSINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å
6 Protein homooligomer Homooligomer Protein × 90 PDB declaration: 90-meric(90) Consistent with protein copy count Chain 0; UniProt 1–340 Chain 1; UniProt 579–880 Chain 3; UniProt 341–578 Not recorded MYR MYRISTIC ACID × 30 SPH SPHINGOSINE × 30 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 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 245 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLH_POL1M
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain 0; PDBConstruct 1–340; UniProt 1–340 Author chain 1; PDBConstruct 1–302; UniProt 579–880 Author chain 3; PDBConstruct 1–238; UniProt 341–578

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 1pov

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pov
Deposition date deposition_date1995-08-10
Structure title titleROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION
Keywords keywordsPICORNAVIRUS, Icosahedral virus, Virus; VIRUS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.58
Radius of gyration Rg (electron density) rg_electron28.68
Forward intensity I(0) i0117579000.00
Molecular weight molecular_weight86255.0 kDa
Excluded volume excluded_volume108150 ų
Envelope volume envelope_volume134090 ų
Hydration-shell volume shell_volume38479 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg36.20
Envelope Rg envelope_rg29.30
Shape Rg shape_rg28.67
Total Rg total_rg29.44
Total atoms total_atoms6071
Residues n_residues773
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 dmax95.8
Rg (real space) rg_real29.54
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.1760e+08
I(0) uncertainty (real space) i0_real_error1.8220e+06
Rg (reciprocal space) rg_reciprocal29.56
I(0) (reciprocal space) i0_reciprocal117600000.0000
Solution quality estimate total_estimate0.8194
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22260000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1pov0_
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)
Domain ID domain_idd1pov1_
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)
Domain ID domain_idd1pov3_
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)

CATH v4.4 (4 domains)

Domain ID domain_id1pov001
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology80 — Rhinovirus 14, subunit 4
Homologous superfamily homologous superfamily10 — Picornavirus coat protein VP4
Domain ID domain_id1pov002
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id1pov100
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id1pov300
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (5)

9. Files and Curves (10)