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9uea

Prefusion structure of GX2012 spike glycoprotein

Method: ELECTRON MICROSCOPY Dmax: 163.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Spike glycoprotein

BtTp-BetaCoV/GX2012

UniProt A0A0U1WJZ6

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 7 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 21–1225 Chain B； UniProt 21–1225 Chain C； UniProt 21–1225 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 alpha-L-fucopyranose-(1-6)-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-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.94 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.

Other PDB Difference from Current Entry 9UEA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9V2P Complex structure of GX2012 spike RBD bound to human DPP4 Deposited 2025-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain G 386–594（209 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.40 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0U1WJZ6_BCHK4
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–1205； UniProt 21–1225 Author chain B； PDBConstruct 1–1205； UniProt 21–1225 Author chain C； PDBConstruct 1–1205； UniProt 21–1225

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 9uea

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uea
Deposition date deposition_date2025-04-08
Structure title titlePrefusion structure of GX2012 spike glycoprotein
Keywords keywordsGX2012, spike, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier51.21 Å
Radius of gyration Rg (electron density) rg_electron50.82 Å
Forward intensity I(0) i02211690000.00
Molecular weight molecular_weight393140.0 kDa
Excluded volume excluded_volume491400 ų
Envelope volume envelope_volume691590 ų
Hydration-shell volume shell_volume110910 ų
Envelope diameter envelope_diameter161.8 Å
Shell Rg shell_rg56.11 Å
Envelope Rg envelope_rg50.12 Å
Shape Rg shape_rg50.83 Å
Total Rg total_rg50.95 Å
Total atoms total_atoms27661
Residues n_residues3509
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax163.4 Å
Rg (real space) rg_real51.08 Å
Rg uncertainty (real space) rg_real_error1.08 Å
I(0) (real space) i0_real2.2120e+09
I(0) uncertainty (real space) i0_real_error3.9920e+07
Rg (reciprocal space) rg_reciprocal51.31 Å
I(0) (reciprocal space) i0_reciprocal2212000000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.0 Å
Skewness Skewness skewness0.210
Kurtosis Kurtosis kurtosis-0.561
Angular range angular_range— – 0.1550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha359400000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.748
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)