8y7y

Local structure of HCoV-HKU1A spike in complex with TMPRSS2 and glycan

Method: ELECTRON MICROSCOPY Dmax: 142.4 Å Quality: GOOD

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

Spike glycoprotein

Human coronavirus HKU1 (isolate N1)

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 Heteromer Protein × 3 其他Polymer 8 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–1281 Chain B; UniProt 14–1281 Not recorded Transmembrane protease serine 2 × 1 (O15393) ;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 ; × 2 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 × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MJJ methyl 9-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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 1–1268; UniProt 14–1281 Author chain B; PDBConstruct 1–1268; UniProt 14–1281

Transmembrane protease serine 2

Homo sapiens

UniProt O15393

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 Heteromer Protein × 3 其他Polymer 8 PDB declaration: trimeric(3) Consistent with protein copy count Chain T; UniProt 109–492 Not recorded Spike glycoprotein × 2 (Q5MQD0) ;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 ; × 2 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 × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MJJ methyl 9-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.24 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.

33 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TMPS2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain T; PDBConstruct 1–383; UniProt 109–492

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 8y7y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y7y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8y7y
Deposition date deposition_date2024-02-05
Structure title titleLocal structure of HCoV-HKU1A spike in complex with TMPRSS2 and glycan
Keywords keywordsHKU1A, spike, TMPRSS2, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.12
Radius of gyration Rg (electron density) rg_electron43.91
Forward intensity I(0) i0146289000.00
Molecular weight molecular_weight97457.0 kDa
Excluded volume excluded_volume121240 ų
Envelope volume envelope_volume181940 ų
Hydration-shell volume shell_volume37964 ų
Envelope diameter envelope_diameter150.0
Shell Rg shell_rg43.77
Envelope Rg envelope_rg43.17
Shape Rg shape_rg43.97
Total Rg total_rg43.71
Total atoms total_atoms6860
Residues n_residues861
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 dmax142.4
Rg (real space) rg_real43.65
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.4630e+08
I(0) uncertainty (real space) i0_real_error2.7800e+06
Rg (reciprocal space) rg_reciprocal43.12
I(0) (reciprocal space) i0_reciprocal146200000.0000
Solution quality estimate total_estimate0.7703
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9615000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.643; Smooth: 0.081

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)