6xyo

Multiple system atrophy Type I alpha-synuclein filament

Method: ELECTRON MICROSCOPY Dmax: 103.7 Å Quality: GOOD

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

Alpha-synuclein

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–140 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 Chain H; UniProt 1–140 Chain I; UniProt 1–140 Chain J; UniProt 1–140 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 A; PDBConstruct 1–140; UniProt 1–140 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 Author chain H; PDBConstruct 1–140; UniProt 1–140 Author chain I; PDBConstruct 1–140; UniProt 1–140 Author chain J; 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 6xyo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xyo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xyo
Deposition date deposition_date2020-01-30
Structure title titleMultiple system atrophy Type I alpha-synuclein filament
Keywords keywordsmultiple system atrophy, alpha-synuclein filament, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.91
Radius of gyration Rg (electron density) rg_electron31.47
Forward intensity I(0) i095837600.00
Molecular weight molecular_weight78134.0 kDa
Excluded volume excluded_volume98481 ų
Envelope volume envelope_volume124740 ų
Hydration-shell volume shell_volume33899 ų
Envelope diameter envelope_diameter104.0
Shell Rg shell_rg37.53
Envelope Rg envelope_rg31.48
Shape Rg shape_rg31.44
Total Rg total_rg32.08
Total atoms total_atoms5490
Residues n_residues800
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 dmax103.7
Rg (real space) rg_real31.97
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real9.5840e+07
I(0) uncertainty (real space) i0_real_error1.5440e+06
Rg (reciprocal space) rg_reciprocal31.95
I(0) (reciprocal space) i0_reciprocal95840000.0000
Solution quality estimate total_estimate0.8960
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.641
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13660000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)