9je8

The cryo-EM structure of Ac-G51DA53T 30days a-syn fibril.

Method: ELECTRON MICROSCOPY Dmax: 90.0 Å Quality: GOOD

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

Alpha-synuclein

Homo sapiens

UniProt P37840

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–140 Chain C; UniProt 1–140 Chain D; UniProt 1–140 Chain E; UniProt 1–140 Chain F; UniProt 1–140 Chain G; UniProt 1–140 Mutation:G51D,A53T No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

226 other PDB entries and 234 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYUA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–140; UniProt 1–140 Author chain C; PDBConstruct 1–140; UniProt 1–140 Author chain D; PDBConstruct 1–140; UniProt 1–140 Author chain E; PDBConstruct 1–140; UniProt 1–140 Author chain F; PDBConstruct 1–140; UniProt 1–140 Author chain G; PDBConstruct 1–140; UniProt 1–140

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 9je8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9je8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9je8
Deposition date deposition_date2024-09-02
Structure title titleThe cryo-EM structure of Ac-G51DA53T 30days a-syn fibril.
Keywords keywordsPROTEIN FIBRIL, amyloid; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.89
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i021500600.00
Molecular weight molecular_weight36438.0 kDa
Excluded volume excluded_volume46261 ų
Envelope volume envelope_volume60709 ų
Hydration-shell volume shell_volume19711 ų
Envelope diameter envelope_diameter95.6
Shell Rg shell_rg32.32
Envelope Rg envelope_rg28.24
Shape Rg shape_rg28.25
Total Rg total_rg28.76
Total atoms total_atoms2562
Residues n_residues366
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 dmax90.0
Rg (real space) rg_real27.97
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.1500e+07
I(0) uncertainty (real space) i0_real_error3.0850e+05
Rg (reciprocal space) rg_reciprocal27.95
I(0) (reciprocal space) i0_reciprocal21500000.0000
Solution quality estimate total_estimate0.8223
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.648
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1077000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.874; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)