7q3u

Cryo-EM structure of TDP43 core peptide amyloid fiber

Method: ELECTRON MICROSCOPY Dmax: 66.4 Å Quality: GOOD

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

TAR DNA-binding protein 43

Homo sapiens

UniProt Q13148

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 homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 279–360 Chain B; UniProt 279–360 Chain C; UniProt 279–360 Chain D; UniProt 279–360 Chain E; UniProt 279–360 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

41 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TADBP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 279–360 Author chain B; PDBConstruct 1–82; UniProt 279–360 Author chain C; PDBConstruct 1–82; UniProt 279–360 Author chain D; PDBConstruct 1–82; UniProt 279–360 Author chain E; PDBConstruct 1–82; UniProt 279–360

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 7q3u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q3u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q3u
Deposition date deposition_date2021-10-28
Structure title titleCryo-EM structure of TDP43 core peptide amyloid fiber
Keywords keywordsTDP-43, Amyloid, Neurodegeneration, Helical, Cryo-EM, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier19.99
Radius of gyration Rg (electron density) rg_electron19.47
Forward intensity I(0) i025730300.00
Molecular weight molecular_weight33927.0 kDa
Excluded volume excluded_volume40212 ų
Envelope volume envelope_volume45882 ų
Hydration-shell volume shell_volume19790 ų
Envelope diameter envelope_diameter67.1
Shell Rg shell_rg25.77
Envelope Rg envelope_rg19.83
Shape Rg shape_rg19.53
Total Rg total_rg20.00
Total atoms total_atoms2355
Residues n_residues355
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 dmax66.4
Rg (real space) rg_real19.97
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.5730e+07
I(0) uncertainty (real space) i0_real_error3.5100e+05
Rg (reciprocal space) rg_reciprocal19.97
I(0) (reciprocal space) i0_reciprocal25730000.0000
Solution quality estimate total_estimate0.8873
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9340000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)