8y87

Structure of HCoV-HKU1C spike in the functionally anchored-1up conformation with 1TMPRSS2

Method: ELECTRON MICROSCOPY Dmax: 210.2 Å Quality: GOOD

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

Spike glycoprotein

Human coronavirus HKU1 (isolate N5)

UniProt Q0ZME7

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 × 4 其他Polymer 3 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 14–1276 Chain B; UniProt 14–1276 Chain C; UniProt 14–1276 Not recorded Transmembrane protease serine 2 × 1 (O15393) 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 × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 22 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHN5
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1263; UniProt 14–1276 Author chain B; PDBConstruct 1–1263; UniProt 14–1276 Author chain C; PDBConstruct 1–1263; UniProt 14–1276

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 × 4 其他Polymer 3 PDB declaration: tetrameric(4) Consistent with protein copy count Chain T; UniProt 109–492 Not recorded Spike glycoprotein × 3 (Q0ZME7) 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 × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 22 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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 8y87

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y87
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8y87
Deposition date deposition_date2024-02-06
Structure title titleStructure of HCoV-HKU1C spike in the functionally anchored-1up conformation with 1TMPRSS2
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_guinier59.14
Radius of gyration Rg (electron density) rg_electron59.55
Forward intensity I(0) i02476770000.00
Molecular weight molecular_weight419320.0 kDa
Excluded volume excluded_volume524710 ų
Envelope volume envelope_volume818160 ų
Hydration-shell volume shell_volume118850 ų
Envelope diameter envelope_diameter233.8
Shell Rg shell_rg58.95
Envelope Rg envelope_rg59.48
Shape Rg shape_rg59.54
Total Rg total_rg59.57
Total atoms total_atoms29520
Residues n_residues3778
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 dmax210.2
Rg (real space) rg_real59.51
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real2.4760e+09
I(0) uncertainty (real space) i0_real_error5.7910e+07
Rg (reciprocal space) rg_reciprocal58.78
I(0) (reciprocal space) i0_reciprocal2474000000.0000
Solution quality estimate total_estimate0.8395
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.3
Skewness Skewness skewness0.662
Kurtosis Kurtosis kurtosis0.432
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0029
Highest regularization parameter α highest_alpha255100000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.709; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)