8xz6

MERS-CoV S and radixin complex structure

Method: X-RAY DIFFRACTION Dmax: 148.8 Å Quality: GOOD

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

Radixin

Homo sapiens

UniProt P35241

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–296 Not recorded ;Spike protein S2' ; × 1 (K9N5Q8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–296 Not recorded ;Spike protein S2' ; × 1 (K9N5Q8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–296 Not recorded ;Spike protein S2' ; × 1 (K9N5Q8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–296 Not recorded ;Spike protein S2' ; × 1 (K9N5Q8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RADI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–298; UniProt 1–296 Author chain B; PDBConstruct 3–298; UniProt 1–296 Author chain C; PDBConstruct 3–298; UniProt 1–296 Author chain D; PDBConstruct 3–298; UniProt 1–296

;Spike protein S2' ;

OrganismNot specified

UniProt K9N5Q8

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1334–1346 Not recorded Radixin × 1 (P35241) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1334–1346 Not recorded Radixin × 1 (P35241) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1334–1346 Not recorded Radixin × 1 (P35241) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1334–1346 Not recorded Radixin × 1 (P35241) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;0.1 M Tris, pH 8.5, and 6% PEG 8000 Resolution 2.12 Å R-free 0.256

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.

12 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_MERS1
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–13; UniProt 1334–1346 Author chain F; PDBConstruct 1–13; UniProt 1334–1346 Author chain G; PDBConstruct 1–13; UniProt 1334–1346 Author chain H; PDBConstruct 1–13; UniProt 1334–1346

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 8xz6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xz6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xz6
Deposition date deposition_date2024-01-20
Structure title titleMERS-CoV S and radixin complex structure
Keywords keywordsMERS-CoV, S, ezrin-radixin-moesin, cytoskeleton, assembly, VIRAL PROTEIN/PROTEIN BINDING, VIRAL PROTEIN-PROTEIN BINDING complex; VIRAL PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.40
Radius of gyration Rg (electron density) rg_electron44.36
Forward intensity I(0) i0283357000.00
Molecular weight molecular_weight143010.0 kDa
Excluded volume excluded_volume181040 ų
Envelope volume envelope_volume271580 ų
Hydration-shell volume shell_volume52938 ų
Envelope diameter envelope_diameter156.7
Shell Rg shell_rg47.51
Envelope Rg envelope_rg42.89
Shape Rg shape_rg44.34
Total Rg total_rg44.61
Total atoms total_atoms10107
Residues n_residues1215
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 dmax148.8
Rg (real space) rg_real44.43
Rg uncertainty (real space) rg_real_error1.67
I(0) (real space) i0_real2.8340e+08
I(0) uncertainty (real space) i0_real_error5.5310e+06
Rg (reciprocal space) rg_reciprocal44.40
I(0) (reciprocal space) i0_reciprocal283300000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.6
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19660000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)