1wnc

Crystal structure of the SARS-CoV Spike protein fusion core

Method: X-RAY DIFFRACTION Dmax: 100.4 Å Quality: GOOD

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

E2 glycoprotein

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 A; UniProt 900–948 Chain A; UniProt 1144–1185 Chain B; UniProt 900–948 Chain B; UniProt 1144–1185 Chain C; UniProt 900–948 Chain C; UniProt 1144–1185 Chain D; UniProt 900–948 Chain D; UniProt 1144–1185 Chain E; UniProt 900–948 Chain E; UniProt 1144–1185 Chain F; UniProt 900–948 Chain F; UniProt 1144–1185 Fragment:residues 900-1184 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 2.5;291 K;PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.273
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 900–948 Chain A; UniProt 1144–1185 Chain B; UniProt 900–948 Chain B; UniProt 1144–1185 Chain C; UniProt 900–948 Chain C; UniProt 1144–1185 Fragment:residues 900-1184 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 2.5;291 K;PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.273
3 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 900–948 Chain D; UniProt 1144–1185 Chain E; UniProt 900–948 Chain E; UniProt 1144–1185 Chain F; UniProt 900–948 Chain F; UniProt 1144–1185 Fragment:residues 900-1184 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 2.5;291 K;PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.80 Å R-free 0.273

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 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGL2_CVHSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–49; UniProt 900–948 Author chain A; PDBConstruct 71–112; UniProt 1144–1185 Author chain B; PDBConstruct 1–49; UniProt 900–948 Author chain B; PDBConstruct 71–112; UniProt 1144–1185 Author chain C; PDBConstruct 1–49; UniProt 900–948 Author chain C; PDBConstruct 71–112; UniProt 1144–1185 Author chain D; PDBConstruct 1–49; UniProt 900–948 Author chain D; PDBConstruct 71–112; UniProt 1144–1185 Author chain E; PDBConstruct 1–49; UniProt 900–948 Author chain E; PDBConstruct 71–112; UniProt 1144–1185 Author chain F; PDBConstruct 1–49; UniProt 900–948 Author chain F; PDBConstruct 71–112; UniProt 1144–1185

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 1wnc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wnc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wnc
Deposition date deposition_date2004-07-29
Structure title titleCrystal structure of the SARS-CoV Spike protein fusion core
Keywords keywordsSARS-CoV, Spike protein, Fusion Core, Heptad repeat, 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_guinier28.57
Radius of gyration Rg (electron density) rg_electron28.42
Forward intensity I(0) i042815100.00
Molecular weight molecular_weight49544.0 kDa
Excluded volume excluded_volume61588 ų
Envelope volume envelope_volume82641 ų
Hydration-shell volume shell_volume25217 ų
Envelope diameter envelope_diameter104.5
Shell Rg shell_rg33.77
Envelope Rg envelope_rg29.02
Shape Rg shape_rg28.41
Total Rg total_rg28.99
Total atoms total_atoms3480
Residues n_residues454
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 dmax100.4
Rg (real space) rg_real28.77
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real4.2820e+07
I(0) uncertainty (real space) i0_real_error7.2500e+05
Rg (reciprocal space) rg_reciprocal28.71
I(0) (reciprocal space) i0_reciprocal42810000.0000
Solution quality estimate total_estimate0.8277
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21730000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.695; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1wnca_
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
Domain ID domain_idd1wncb_
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
Domain ID domain_idd1wncc_
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
Domain ID domain_idd1wncd_
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
Domain ID domain_idd1wnce_
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
Domain ID domain_idd1wncf_
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 (6 domains)

Domain ID domain_id1wncA00
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_id1wncB00
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_id1wncC00
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_id1wncD00
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_id1wncE00
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_id1wncF00
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

8. Citations (1)

9. Files and Curves (10)