7vym

Coxsackievirus B3 at pH7.4 (VP3-234E) incubation with coxsackievirus and adenovirus receptor for 10min

Method: ELECTRON MICROSCOPY Dmax: 97.5 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 3.68 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 3.68 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 3.68 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 3.68 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 3.68 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 7vym

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7vym
Deposition date deposition_date2021-11-14
Structure title titleCoxsackievirus B3 at pH7.4 (VP3-234E) incubation with coxsackievirus and adenovirus receptor for 10min
Keywords keywordsCVB3, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.97
Radius of gyration Rg (electron density) rg_electron30.01
Forward intensity I(0) i0165114000.00
Molecular weight molecular_weight101810.0 kDa
Excluded volume excluded_volume127100 ų
Envelope volume envelope_volume159010 ų
Hydration-shell volume shell_volume43013 ų
Envelope diameter envelope_diameter105.8
Shell Rg shell_rg38.16
Envelope Rg envelope_rg30.64
Shape Rg shape_rg29.99
Total Rg total_rg30.76
Total atoms total_atoms7162
Residues n_residues921
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 dmax97.5
Rg (real space) rg_real30.89
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.6510e+08
I(0) uncertainty (real space) i0_real_error2.4310e+06
Rg (reciprocal space) rg_reciprocal30.93
I(0) (reciprocal space) i0_reciprocal165100000.0000
Solution quality estimate total_estimate0.8995
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29720000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.916

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_id7vymB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)