6l4s

cryo-em structure of alpha-synuclein fiber mutation type E46K

Method: ELECTRON MICROSCOPY Dmax: 97.2 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 A; UniProt 45–99 Chain B; UniProt 45–99 Chain C; UniProt 45–99 Chain D; UniProt 45–99 Chain E; UniProt 45–99 Chain F; UniProt 45–99 Mutation:E46K No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 1–55; UniProt 45–99 Author chain B; PDBConstruct 1–55; UniProt 45–99 Author chain C; PDBConstruct 1–55; UniProt 45–99 Author chain D; PDBConstruct 1–55; UniProt 45–99 Author chain E; PDBConstruct 1–55; UniProt 45–99 Author chain F; PDBConstruct 1–55; UniProt 45–99

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 6l4s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6l4s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6l4s
Deposition date deposition_date2019-10-21
Structure title titlecryo-em structure of alpha-synuclein fiber mutation type E46K
Keywords keywordsalpha-syn fiber, Parkinson disease, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.29
Radius of gyration Rg (electron density) rg_electron26.22
Forward intensity I(0) i017768400.00
Molecular weight molecular_weight32281.0 kDa
Excluded volume excluded_volume40771 ų
Envelope volume envelope_volume53033 ų
Hydration-shell volume shell_volume18527 ų
Envelope diameter envelope_diameter100.7
Shell Rg shell_rg30.64
Envelope Rg envelope_rg27.02
Shape Rg shape_rg26.19
Total Rg total_rg26.90
Total atoms total_atoms2268
Residues n_residues330
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 dmax97.2
Rg (real space) rg_real26.53
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real1.7770e+07
I(0) uncertainty (real space) i0_real_error3.1810e+05
Rg (reciprocal space) rg_reciprocal26.46
I(0) (reciprocal space) i0_reciprocal17770000.0000
Solution quality estimate total_estimate0.8208
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis-0.171
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1375000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.544; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)