9bsw

Cryo-EM structure of HCoV-HKU1 Spike glycoprotein (DDA state)

Method: ELECTRON MICROSCOPY Dmax: 164.9 Å Quality: GOOD

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

Spike glycoprotein

Human coronavirus HKU1

UniProt Q5MQD0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 3 其他Polymer 23 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–1298 Chain B; UniProt 14–1298 Chain C; UniProt 14–1298 Fragment:ectodomain (UNP residues 14-1298) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 18 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 36 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.06 Å

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.

30 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHN1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1285; UniProt 14–1298 Author chain B; PDBConstruct 1–1285; UniProt 14–1298 Author chain C; PDBConstruct 1–1285; UniProt 14–1298

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 9bsw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bsw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bsw
Deposition date deposition_date2024-05-14
Structure title titleCryo-EM structure of HCoV-HKU1 Spike glycoprotein (DDA state)
Keywords keywordsHCoV-HKU1 spike glycoprotein ectodomain, proline stablized, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.10
Radius of gyration Rg (electron density) rg_electron50.65
Forward intensity I(0) i02481100000.00
Molecular weight molecular_weight417870.0 kDa
Excluded volume excluded_volume522380 ų
Envelope volume envelope_volume718830 ų
Hydration-shell volume shell_volume114210 ų
Envelope diameter envelope_diameter166.9
Shell Rg shell_rg57.05
Envelope Rg envelope_rg50.09
Shape Rg shape_rg50.62
Total Rg total_rg50.93
Total atoms total_atoms29387
Residues n_residues3582
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 dmax164.9
Rg (real space) rg_real50.95
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real2.4810e+09
I(0) uncertainty (real space) i0_real_error3.6710e+07
Rg (reciprocal space) rg_reciprocal51.22
I(0) (reciprocal space) i0_reciprocal2482000000.0000
Solution quality estimate total_estimate0.8219
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.5
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha294800000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)