8vgt

Structure of the HKU1 RBD bound to the human TMPRSS2 receptor

Method: ELECTRON MICROSCOPY Dmax: 115.1 Å Quality: GOOD

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

Spike protein S1

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 320–614 Fragment:RBD Transmembrane protease serine 2 × 1 (O15393) 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 × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 33–327; UniProt 320–614

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 109–492 Not recorded Spike protein S1 × 1 (Q5MQD0) 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 × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 B; PDBConstruct 19–401; 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 8vgt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vgt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8vgt
Deposition date deposition_date2023-12-27
Structure title titleStructure of the HKU1 RBD bound to the human TMPRSS2 receptor
Keywords keywords;Spike glycoprotein, fusion protein, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, inhibitor, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.66
Radius of gyration Rg (electron density) rg_electron34.57
Forward intensity I(0) i073263600.00
Molecular weight molecular_weight67001.0 kDa
Excluded volume excluded_volume83094 ų
Envelope volume envelope_volume111690 ų
Hydration-shell volume shell_volume28273 ų
Envelope diameter envelope_diameter120.5
Shell Rg shell_rg38.88
Envelope Rg envelope_rg34.25
Shape Rg shape_rg34.59
Total Rg total_rg34.83
Total atoms total_atoms4714
Residues n_residues629
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 dmax115.1
Rg (real space) rg_real34.90
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real7.3260e+07
I(0) uncertainty (real space) i0_real_error1.2970e+06
Rg (reciprocal space) rg_reciprocal34.75
I(0) (reciprocal space) i0_reciprocal73250000.0000
Solution quality estimate total_estimate0.8285
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.740
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8667000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.665; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)