5ktz

expanded poliovirus in complex with VHH 12B

Method: ELECTRON MICROSCOPY Dmax: 100.6 Å Quality: EXCELLENT

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

VP1

Poliovirus type 1 (strain 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 × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain 1; UniProt 636–858 Chain 2; UniProt 70–338 Chain 3; UniProt 342–572 Fragment:UNP residues 636-858 Fragment:UNP residues 70-338 Fragment:UNP residues 342-572 VHH 12B × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 1; UniProt 636–858 Chain 2; UniProt 70–338 Chain 3; UniProt 342–572 Fragment:UNP residues 636-858 Fragment:UNP residues 70-338 Fragment:UNP residues 342-572 VHH 12B × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å
3 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain 1; UniProt 636–858 Chain 2; UniProt 70–338 Chain 3; UniProt 342–572 Fragment:UNP residues 636-858 Fragment:UNP residues 70-338 Fragment:UNP residues 342-572 VHH 12B × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 1; UniProt 636–858 Chain 2; UniProt 70–338 Chain 3; UniProt 342–572 Fragment:UNP residues 636-858 Fragment:UNP residues 70-338 Fragment:UNP residues 342-572 VHH 12B × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 1; UniProt 636–858 Chain 2; UniProt 70–338 Chain 3; UniProt 342–572 Fragment:UNP residues 636-858 Fragment:UNP residues 70-338 Fragment:UNP residues 342-572 VHH 12B × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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, 3
Chains and sequence ranges Author chain 1; PDBConstruct 1–223; UniProt 636–858 Author chain 2; PDBConstruct 1–269; UniProt 70–338 Author chain 3; PDBConstruct 1–231; UniProt 342–572

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 5ktz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ktz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ktz
Deposition date deposition_date2016-07-12
Structure title titleexpanded poliovirus in complex with VHH 12B
Keywords keywordspoliovirus, VHH, nanobody, 80S, expanded, single domain antibody, VIRUS-immune system complex; VIRUS/immune system
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.53
Radius of gyration Rg (electron density) rg_electron30.74
Forward intensity I(0) i0127330000.00
Molecular weight molecular_weight89182.0 kDa
Excluded volume excluded_volume111370 ų
Envelope volume envelope_volume144070 ų
Hydration-shell volume shell_volume39234 ų
Envelope diameter envelope_diameter110.9
Shell Rg shell_rg37.46
Envelope Rg envelope_rg31.18
Shape Rg shape_rg30.73
Total Rg total_rg31.37
Total atoms total_atoms6276
Residues n_residues805
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 dmax100.6
Rg (real space) rg_real31.50
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.2730e+08
I(0) uncertainty (real space) i0_real_error1.9790e+06
Rg (reciprocal space) rg_reciprocal31.52
I(0) (reciprocal space) i0_reciprocal127300000.0000
Solution quality estimate total_estimate0.9045
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.2
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25300000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)