1zvb

A structure-based mechanism of SARS virus membrane fusion

Method: X-RAY DIFFRACTION Dmax: 57.7 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 940–973 Chain B; UniProt 940–973 Chain C; UniProt 940–973 Fragment:residues 940-973 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;PEG 4000, isopropanol, sodium citrate, pH 5.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.239

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
Chains and sequence ranges Author chain A; PDBConstruct 1–34; UniProt 940–973 Author chain B; PDBConstruct 1–34; UniProt 940–973 Author chain C; PDBConstruct 1–34; UniProt 940–973

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 1zvb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1zvb
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_guinier16.82
Radius of gyration Rg (electron density) rg_electron16.24
Forward intensity I(0) i02313280.00
Molecular weight molecular_weight10861.0 kDa
Excluded volume excluded_volume13764 ų
Envelope volume envelope_volume16396 ų
Hydration-shell volume shell_volume9594 ų
Envelope diameter envelope_diameter55.7
Shell Rg shell_rg20.16
Envelope Rg envelope_rg16.69
Shape Rg shape_rg16.20
Total Rg total_rg17.19
Total atoms total_atoms763
Residues n_residues101
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 dmax57.7
Rg (real space) rg_real16.97
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.3130e+06
I(0) uncertainty (real space) i0_real_error2.6800e+04
Rg (reciprocal space) rg_reciprocal16.95
I(0) (reciprocal space) i0_reciprocal2313000.0000
Solution quality estimate total_estimate0.7580
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.7
Skewness Skewness skewness0.546
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha465800.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.324; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1zvba1
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_idd1zvbb_
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_idd1zvbc_
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

8. Citations (1)

9. Files and Curves (10)