9daz

Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. Complex of fAPN with FCoV-23 RBD

Method: ELECTRON MICROSCOPY Dmax: 159.3 Å Quality: GOOD

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

Aminopeptidase N,Immunoglobulin gamma-1 heavy chain

Felis catus

UniProt P0DOX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 其他Polymer 12 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 218–449 Chain C; UniProt 218–449 Not recorded Spike glycoprotein × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 953–1184; UniProt 218–449 Author chain C; PDBConstruct 953–1184; UniProt 218–449

Aminopeptidase N,Immunoglobulin gamma-1 heavy chain

Felis catus

UniProt P79171

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 其他Polymer 12 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 64–967 Chain C; UniProt 64–967 Not recorded Spike glycoprotein × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.50 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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMPN_FELCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 33–936; UniProt 64–967 Author chain C; PDBConstruct 33–936; UniProt 64–967

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 9daz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9daz
Deposition date deposition_date2024-08-23
Structure title titleMolecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. Complex of fAPN with FCoV-23 RBD
Keywords keywords;Coronavirus, alphacoronavirus, feline coronavirus, cryo-EM, neutralization assays, binding assays, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, VIRAL PROTEIN-HYDROLASE complex ;; VIRAL PROTEIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.87
Radius of gyration Rg (electron density) rg_electron46.87
Forward intensity I(0) i0617652000.00
Molecular weight molecular_weight209770.0 kDa
Excluded volume excluded_volume263750 ų
Envelope volume envelope_volume373520 ų
Hydration-shell volume shell_volume68812 ų
Envelope diameter envelope_diameter160.5
Shell Rg shell_rg49.11
Envelope Rg envelope_rg45.87
Shape Rg shape_rg46.89
Total Rg total_rg46.92
Total atoms total_atoms14854
Residues n_residues1926
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 dmax159.3
Rg (real space) rg_real47.06
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real6.1770e+08
I(0) uncertainty (real space) i0_real_error1.2760e+07
Rg (reciprocal space) rg_reciprocal46.87
I(0) (reciprocal space) i0_reciprocal617500000.0000
Solution quality estimate total_estimate0.8045
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.386
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64460000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)