7dpf

Cryo-EM structure of Coxsackievirus B1 mature virion

Method: ELECTRON MICROSCOPY Dmax: 99.2 Å Quality: REASONABLE

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

Virion protein 1

OrganismNot specified

UniProt W8GTF7

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 1–278 Not recorded VP2 × 60 (A0A2S0RQC2) VP3 × 60 (A0A0G4PYT0) Capsid protein VP4 × 60 (A0A2S1FMR1) PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 1; UniProt 1–278 Not recorded VP2 × 1 (A0A2S0RQC2) VP3 × 1 (A0A0G4PYT0) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain 1; UniProt 1–278 Not recorded VP2 × 5 (A0A2S0RQC2) VP3 × 5 (A0A0G4PYT0) Capsid protein VP4 × 5 (A0A2S1FMR1) PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 1; UniProt 1–278 Not recorded VP2 × 6 (A0A2S0RQC2) VP3 × 6 (A0A0G4PYT0) Capsid protein VP4 × 6 (A0A2S1FMR1) PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 1; UniProt 1–278 Not recorded VP2 × 1 (A0A2S0RQC2) VP3 × 1 (A0A0G4PYT0) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

25 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W8GTF7_9ENTO
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–278; UniProt 1–278

VP2

OrganismNot specified

UniProt A0A2S0RQC2

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 2; UniProt 70–332 Not recorded Virion protein 1 × 60 (W8GTF7) VP3 × 60 (A0A0G4PYT0) Capsid protein VP4 × 60 (A0A2S1FMR1) PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 2; UniProt 70–332 Not recorded Virion protein 1 × 1 (W8GTF7) VP3 × 1 (A0A0G4PYT0) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain 2; UniProt 70–332 Not recorded Virion protein 1 × 5 (W8GTF7) VP3 × 5 (A0A0G4PYT0) Capsid protein VP4 × 5 (A0A2S1FMR1) PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 2; UniProt 70–332 Not recorded Virion protein 1 × 6 (W8GTF7) VP3 × 6 (A0A0G4PYT0) Capsid protein VP4 × 6 (A0A2S1FMR1) PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 2; UniProt 70–332 Not recorded Virion protein 1 × 1 (W8GTF7) VP3 × 1 (A0A0G4PYT0) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

23 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2S0RQC2_9ENTO
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–263; UniProt 70–332

VP3

OrganismNot specified

UniProt A0A0G4PYT0

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 3; UniProt 333–570 Not recorded Virion protein 1 × 60 (W8GTF7) VP2 × 60 (A0A2S0RQC2) Capsid protein VP4 × 60 (A0A2S1FMR1) PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 3; UniProt 333–570 Not recorded Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain 3; UniProt 333–570 Not recorded Virion protein 1 × 5 (W8GTF7) VP2 × 5 (A0A2S0RQC2) Capsid protein VP4 × 5 (A0A2S1FMR1) PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 3; UniProt 333–570 Not recorded Virion protein 1 × 6 (W8GTF7) VP2 × 6 (A0A2S0RQC2) Capsid protein VP4 × 6 (A0A2S1FMR1) PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 3; UniProt 333–570 Not recorded Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) Capsid protein VP4 × 1 (A0A2S1FMR1) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

1 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G4PYT0_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–238; UniProt 333–570

Capsid protein VP4

OrganismNot specified

UniProt A0A2S1FMR1

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 4; UniProt 1–69 Not recorded Virion protein 1 × 60 (W8GTF7) VP2 × 60 (A0A2S0RQC2) VP3 × 60 (A0A0G4PYT0) PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 4; UniProt 1–69 Not recorded Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) VP3 × 1 (A0A0G4PYT0) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
3 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain 4; UniProt 1–69 Not recorded Virion protein 1 × 5 (W8GTF7) VP2 × 5 (A0A2S0RQC2) VP3 × 5 (A0A0G4PYT0) PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
4 Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain 4; UniProt 1–69 Not recorded Virion protein 1 × 6 (W8GTF7) VP2 × 6 (A0A2S0RQC2) VP3 × 6 (A0A0G4PYT0) PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain 4; UniProt 1–69 Not recorded Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) VP3 × 1 (A0A0G4PYT0) PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

14 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2S1FMR1_9ENTO
Isoform
PDB entities 4
Chains and sequence ranges Author chain 4; PDBConstruct 1–69; UniProt 1–69

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 7dpf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7dpf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7dpf
Deposition date deposition_date2020-12-18
Structure title titleCryo-EM structure of Coxsackievirus B1 mature virion
Keywords keywordsCoxsackievirus B1, mature virion, Cryo-EM, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.25
Radius of gyration Rg (electron density) rg_electron29.23
Forward intensity I(0) i0133287000.00
Molecular weight molecular_weight90409.0 kDa
Excluded volume excluded_volume112680 ų
Envelope volume envelope_volume147220 ų
Hydration-shell volume shell_volume41202 ų
Envelope diameter envelope_diameter104.3
Shell Rg shell_rg37.07
Envelope Rg envelope_rg29.87
Shape Rg shape_rg29.21
Total Rg total_rg29.99
Total atoms total_atoms6354
Residues n_residues810
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 dmax99.2
Rg (real space) rg_real30.21
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.3330e+08
I(0) uncertainty (real space) i0_real_error1.9260e+06
Rg (reciprocal space) rg_reciprocal30.23
I(0) (reciprocal space) i0_reciprocal133300000.0000
Solution quality estimate total_estimate0.6713
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.2
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26610000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 0.077; Positv: 1.000; Valcen: 1.000; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7dpf201
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)