9btc

Cryo-EM density map of HKU1 spike glycoprotein D1 domain in complex with 9O-acetyl GD3 sialoglycan (Up state, locally refined)

Method: ELECTRON MICROSCOPY Dmax: 74.6 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 Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 14–1223 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 ; × 1 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 × 6 A1AR1 5-acetamido-8-O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.41 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 1–1194; UniProt 14–1223

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 9btc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9btc
Deposition date deposition_date2024-05-14
Structure title titleCryo-EM density map of HKU1 spike glycoprotein D1 domain in complex with 9O-acetyl GD3 sialoglycan (Up state, locally refined)
Keywords keywordsHKU1 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_guinier20.53
Radius of gyration Rg (electron density) rg_electron19.58
Forward intensity I(0) i036017800.00
Molecular weight molecular_weight31776.0 kDa
Excluded volume excluded_volume31194 ų
Envelope volume envelope_volume49954 ų
Hydration-shell volume shell_volume21242 ų
Envelope diameter envelope_diameter78.5
Shell Rg shell_rg26.36
Envelope Rg envelope_rg20.13
Shape Rg shape_rg19.52
Total Rg total_rg20.40
Total atoms total_atoms2409
Residues n_residues268
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 dmax74.6
Rg (real space) rg_real20.50
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real3.6020e+07
I(0) uncertainty (real space) i0_real_error5.0860e+05
Rg (reciprocal space) rg_reciprocal20.50
I(0) (reciprocal space) i0_reciprocal36020000.0000
Solution quality estimate total_estimate0.7558
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.053
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8650000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.620; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)