8qeo

cryo-EM structure complex of Frizzled-7 and Clostridioides difficile toxin B

Method: ELECTRON MICROSCOPY Dmax: 203.5 Å Quality: REASONABLE

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

Toxin B

Clostridioides difficile

UniProt P18177

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–2366 Not recorded Frizzled-7 × 1 (O75084) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;100 mM TRIS-HCl pH 7.5 200 mM NaCl 0.002% LMNG 0.0002% CHS 0.0002% GDN 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 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TCDB_CLODI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–2380; UniProt 1–2366

Frizzled-7

Homo sapiens

UniProt O75084

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 33–574 Not recorded Toxin B × 1 (P18177) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;100 mM TRIS-HCl pH 7.5 200 mM NaCl 0.002% LMNG 0.0002% CHS 0.0002% GDN 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.

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FZD7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 24–565; UniProt 33–574

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 8qeo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qeo
Deposition date deposition_date2023-09-01
Structure title titlecryo-EM structure complex of Frizzled-7 and Clostridioides difficile toxin B
Keywords keywordsmicriobiology, class F G protein-coupled receptors, CROP dynamics, TOXIN; TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.55
Radius of gyration Rg (electron density) rg_electron59.32
Forward intensity I(0) i0930009000.00
Molecular weight molecular_weight256930.0 kDa
Excluded volume excluded_volume322220 ų
Envelope volume envelope_volume496620 ų
Hydration-shell volume shell_volume76956 ų
Envelope diameter envelope_diameter229.0
Shell Rg shell_rg52.68
Envelope Rg envelope_rg59.44
Shape Rg shape_rg59.38
Total Rg total_rg58.91
Total atoms total_atoms18126
Residues n_residues2267
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 dmax203.5
Rg (real space) rg_real59.23
Rg uncertainty (real space) rg_real_error1.62
I(0) (real space) i0_real9.2970e+08
I(0) uncertainty (real space) i0_real_error1.9770e+07
Rg (reciprocal space) rg_reciprocal57.91
I(0) (reciprocal space) i0_reciprocal928000000.0000
Solution quality estimate total_estimate0.5762
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.8
Skewness Skewness skewness0.611
Kurtosis Kurtosis kurtosis-0.166
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0043
Highest regularization parameter α highest_alpha45860000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.811; Smooth: 0.447

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)