2bez

Structure of a proteolitically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein

Method: X-RAY DIFFRACTION Dmax: 112.5 Å Quality: REASONABLE

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

Spike glycoprotein

Human SARS coronavirus

UniProt P59594

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 896–972 Chain F; UniProt 1142–1183 Fragment:RESIDUES 896-972 Fragment:RESIDUES 1142-1183 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1M TRIS-HCL, PH 7.0, 1.8M AMMONIUM SULPHATE, 0.1M NACL Resolution 1.60 Å R-free 0.244

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.

76 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHSA
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain C; PDBConstruct 1–77; UniProt 896–972 Author chain F; PDBConstruct 1–42; UniProt 1142–1183

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 2bez

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bez
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bez
Deposition date deposition_date2004-12-02
Structure title titleStructure of a proteolitically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
Keywords keywordsCOILED COIL, MEMBRANE FUSION, SEVERE ACUTE RESPIRATORY SYNDROME, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.64
Radius of gyration Rg (electron density) rg_electron30.92
Forward intensity I(0) i02977470.00
Molecular weight molecular_weight12161.0 kDa
Excluded volume excluded_volume15047 ų
Envelope volume envelope_volume22869 ų
Hydration-shell volume shell_volume8437 ų
Envelope diameter envelope_diameter117.0
Shell Rg shell_rg27.46
Envelope Rg envelope_rg32.28
Shape Rg shape_rg30.99
Total Rg total_rg30.23
Total atoms total_atoms855
Residues n_residues119
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 dmax112.5
Rg (real space) rg_real30.57
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real2.9770e+06
I(0) uncertainty (real space) i0_real_error5.2030e+04
Rg (reciprocal space) rg_reciprocal30.17
I(0) (reciprocal space) i0_reciprocal2977000.0000
Solution quality estimate total_estimate0.6228
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.9
Skewness Skewness skewness0.693
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110900.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.078; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.008; Smooth: 0.849

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2bez.1
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.3 — Coronavirus S2 glycoprotein
Family Family familyh.3.3.1 — Coronavirus spike glycoprotein S2 fragments

CATH v4.4 (2 domains)

Domain ID domain_id2bezC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily300
Domain ID domain_id2bezF00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily790 — Single helix bin

8. Citations (1)

9. Files and Curves (10)