8e8l

9H2 Fab-poliovirus 1 complex

Method: ELECTRON MICROSCOPY Dmax: 103.0 Å Quality: EXCELLENT

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

Capsid 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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric(360) Consistent with protein copy count Chain 1; UniProt 600–881 Chain 2; UniProt 77–341 Chain 4; UniProt 2–69 Not recorded Capsid protein VP3 × 60 (B0L5R5) 9H2 Fab heavy chain × 60 9H2 Fab light chain × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 600–881 Chain 2; UniProt 77–341 Chain 4; UniProt 2–69 Not recorded Capsid protein VP3 × 1 (B0L5R5) 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 600–881 Chain 2; UniProt 77–341 Chain 4; UniProt 2–69 Not recorded Capsid protein VP3 × 5 (B0L5R5) 9H2 Fab heavy chain × 5 9H2 Fab light chain × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain 1; UniProt 600–881 Chain 2; UniProt 77–341 Chain 4; UniProt 2–69 Not recorded Capsid protein VP3 × 6 (B0L5R5) 9H2 Fab heavy chain × 6 9H2 Fab light chain × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 1; UniProt 600–881 Chain 2; UniProt 77–341 Chain 4; UniProt 2–69 Not recorded Capsid protein VP3 × 1 (B0L5R5) 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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, 4
Chains and sequence ranges Author chain 1; PDBConstruct 1–282; UniProt 600–881 Author chain 2; PDBConstruct 1–265; UniProt 77–341 Author chain 4; PDBConstruct 1–68; UniProt 2–69

Capsid protein VP3

OrganismNot specified

UniProt B0L5R5

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 3; UniProt 342–576 Not recorded Capsid protein VP1 × 60 (P03300) Capsid protein VP2 × 60 (P03300) Capsid protein VP4 × 60 (P03300) 9H2 Fab heavy chain × 60 9H2 Fab light chain × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 3; UniProt 342–576 Not recorded Capsid protein VP1 × 1 (P03300) Capsid protein VP2 × 1 (P03300) Capsid protein VP4 × 1 (P03300) 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 3; UniProt 342–576 Not recorded Capsid protein VP1 × 5 (P03300) Capsid protein VP2 × 5 (P03300) Capsid protein VP4 × 5 (P03300) 9H2 Fab heavy chain × 5 9H2 Fab light chain × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain 3; UniProt 342–576 Not recorded Capsid protein VP1 × 6 (P03300) Capsid protein VP2 × 6 (P03300) Capsid protein VP4 × 6 (P03300) 9H2 Fab heavy chain × 6 9H2 Fab light chain × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 3; UniProt 342–576 Not recorded Capsid protein VP1 × 1 (P03300) Capsid protein VP2 × 1 (P03300) Capsid protein VP4 × 1 (P03300) 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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 B0L5R5_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–235; UniProt 342–576

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 8e8l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e8l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e8l
Deposition date deposition_date2022-08-25
Structure title title9H2 Fab-poliovirus 1 complex
Keywords keywordsComplex, Fab, poliovirus, neutralizing, 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_guinier33.21
Radius of gyration Rg (electron density) rg_electron32.35
Forward intensity I(0) i0218995000.00
Molecular weight molecular_weight118140.0 kDa
Excluded volume excluded_volume147530 ų
Envelope volume envelope_volume191710 ų
Hydration-shell volume shell_volume48108 ų
Envelope diameter envelope_diameter110.3
Shell Rg shell_rg40.32
Envelope Rg envelope_rg32.63
Shape Rg shape_rg32.32
Total Rg total_rg33.07
Total atoms total_atoms8318
Residues n_residues1068
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 dmax103.0
Rg (real space) rg_real33.10
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.1900e+08
I(0) uncertainty (real space) i0_real_error3.1590e+06
Rg (reciprocal space) rg_reciprocal33.15
I(0) (reciprocal space) i0_reciprocal219000000.0000
Solution quality estimate total_estimate0.9017
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.493
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47710000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8e8l201
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id8e8lH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8e8lL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)