6xyp

Multiple system atrophy Type II-1 alpha-synuclein filament

Method: ELECTRON MICROSCOPY Dmax: 100.1 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 3.29 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 6xyp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xyp
Deposition date deposition_date2020-01-30
Structure title titleMultiple system atrophy Type II-1 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_guinier31.02
Radius of gyration Rg (electron density) rg_electron30.53
Forward intensity I(0) i078560900.00
Molecular weight molecular_weight70486.0 kDa
Excluded volume excluded_volume88903 ų
Envelope volume envelope_volume111940 ų
Hydration-shell volume shell_volume31568 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg36.43
Envelope Rg envelope_rg30.71
Shape Rg shape_rg30.52
Total Rg total_rg31.10
Total atoms total_atoms4955
Residues n_residues725
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 dmax100.1
Rg (real space) rg_real31.12
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real7.8560e+07
I(0) uncertainty (real space) i0_real_error1.2450e+06
Rg (reciprocal space) rg_reciprocal31.08
I(0) (reciprocal space) i0_reciprocal78560000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.4
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha11380000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.877; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)