1zv8

A structure-based mechanism of SARS virus membrane fusion

Method: X-RAY DIFFRACTION Dmax: 101.4 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 901–950 Chain B; UniProt 1150–1185 Chain C; UniProt 901–950 Chain D; UniProt 1150–1185 Chain E; UniProt 901–950 Chain F; UniProt 1150–1185 Fragment:residues 901-950 Fragment:residues 1150-1185 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;PEG 8000, zinc acetate, sodium cacodylate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.94 Å R-free 0.274
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 901–950 Chain H; UniProt 1150–1185 Chain I; UniProt 901–950 Chain J; UniProt 1150–1185 Chain K; UniProt 901–950 Chain L; UniProt 1150–1185 Fragment:residues 901-950 Fragment:residues 1150-1185 NA SODIUM ION × 4 CAC CACODYLATE ION × 1 ZN ZINC ION × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;PEG 8000, zinc acetate, sodium cacodylate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.94 Å R-free 0.274

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 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGL2_CVHSA
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–50; UniProt 901–950 Author chain C; PDBConstruct 1–50; UniProt 901–950 Author chain E; PDBConstruct 1–50; UniProt 901–950 Author chain G; PDBConstruct 1–50; UniProt 901–950 Author chain I; PDBConstruct 1–50; UniProt 901–950 Author chain K; PDBConstruct 1–50; UniProt 901–950 Author chain B; PDBConstruct 1–36; UniProt 1150–1185 Author chain D; PDBConstruct 1–36; UniProt 1150–1185 Author chain F; PDBConstruct 1–36; UniProt 1150–1185 Author chain H; PDBConstruct 1–36; UniProt 1150–1185 Author chain J; PDBConstruct 1–36; UniProt 1150–1185 Author chain L; PDBConstruct 1–36; UniProt 1150–1185

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 1zv8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zv8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zv8
Deposition date deposition_date2005-06-01
Structure title titleA structure-based mechanism of SARS virus membrane fusion
Keywords keywordsSARS coronavirus, membrane fusion, S2, virus entry, coiled coils, conformational change, 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_guinier27.85
Radius of gyration Rg (electron density) rg_electron27.08
Forward intensity I(0) i047528700.00
Molecular weight molecular_weight52718.0 kDa
Excluded volume excluded_volume65790 ų
Envelope volume envelope_volume82739 ų
Hydration-shell volume shell_volume26305 ų
Envelope diameter envelope_diameter105.8
Shell Rg shell_rg33.19
Envelope Rg envelope_rg27.30
Shape Rg shape_rg26.96
Total Rg total_rg28.08
Total atoms total_atoms3685
Residues n_residues477
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 dmax101.4
Rg (real space) rg_real27.97
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real4.7530e+07
I(0) uncertainty (real space) i0_real_error7.9160e+05
Rg (reciprocal space) rg_reciprocal27.93
I(0) (reciprocal space) i0_reciprocal47530000.0000
Solution quality estimate total_estimate0.8353
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.6
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.088
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18960000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.826; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1zv8.1
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
Domain ID domain_idd1zv8.2
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_idd1zv8.3
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_idd1zv8.4
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_idd1zv8.5
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_idd1zv8.6
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_id1zv8A00
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_id1zv8C00
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_id1zv8E00
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_id1zv8G00
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_id1zv8I00
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_id1zv8K00
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)