7w14

Coxsackievirus B3 at pH7.4 (VP3-234E) incubation with coxsackievirus and adenovirus receptor for 20min

Method: ELECTRON MICROSCOPY Dmax: 99.5 Å Quality: GOOD

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

Coxsackievirus and adenovirus receptor

Homo sapiens

UniProt P78310

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 × 300 PDB declaration: 300-meric(300) Consistent with protein copy count Chain E; UniProt 21–236 Not recorded Capsid protein VP1 × 60 Capsid protein VP2 × 60 Capsid protein VP3 × 60 Capsid protein VP4 × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 21–236 Not recorded Capsid protein VP1 × 1 Capsid protein VP2 × 1 Capsid protein VP3 × 1 Capsid protein VP4 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain E; UniProt 21–236 Not recorded Capsid protein VP1 × 5 Capsid protein VP2 × 5 Capsid protein VP3 × 5 Capsid protein VP4 × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain E; UniProt 21–236 Not recorded Capsid protein VP1 × 6 Capsid protein VP2 × 6 Capsid protein VP3 × 6 Capsid protein VP4 × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 21–236 Not recorded Capsid protein VP1 × 1 Capsid protein VP2 × 1 Capsid protein VP3 × 1 Capsid protein VP4 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 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.

20 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXAR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 2–217; UniProt 21–236

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 7w14

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w14
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7w14
Deposition date deposition_date2021-11-19
Structure title titleCoxsackievirus B3 at pH7.4 (VP3-234E) incubation with coxsackievirus and adenovirus receptor for 20min
Keywords keywordsCVB3, VP3-234E, coxsackievirus and adenovirus receptor, 20min, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.83
Radius of gyration Rg (electron density) rg_electron30.88
Forward intensity I(0) i0174304000.00
Molecular weight molecular_weight104440.0 kDa
Excluded volume excluded_volume130290 ų
Envelope volume envelope_volume168230 ų
Hydration-shell volume shell_volume44443 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg38.82
Envelope Rg envelope_rg31.32
Shape Rg shape_rg30.86
Total Rg total_rg31.61
Total atoms total_atoms7346
Residues n_residues946
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 dmax99.5
Rg (real space) rg_real31.72
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.7430e+08
I(0) uncertainty (real space) i0_real_error2.5980e+06
Rg (reciprocal space) rg_reciprocal31.77
I(0) (reciprocal space) i0_reciprocal174300000.0000
Solution quality estimate total_estimate0.8997
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30720000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.887

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_id7w14B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)