7v49

Type 4 alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient

Method: ELECTRON MICROSCOPY Dmax: 57.8 Å Quality: REASONABLE

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–140 Chain B; UniProt 1–140 Chain C; UniProt 1–140 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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

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 7v49

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v49
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v49
Deposition date deposition_date2021-08-12
Structure title titleType 4 alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient
Keywords keywordsamyloid fibril, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier20.63
Radius of gyration Rg (electron density) rg_electron20.90
Forward intensity I(0) i05491170.00
Molecular weight molecular_weight17354.0 kDa
Excluded volume excluded_volume21959 ų
Envelope volume envelope_volume27751 ų
Hydration-shell volume shell_volume12777 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg24.66
Envelope Rg envelope_rg21.18
Shape Rg shape_rg20.90
Total Rg total_rg21.56
Total atoms total_atoms1221
Residues n_residues180
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 dmax57.8
Rg (real space) rg_real19.72
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real5.2790e+06
I(0) uncertainty (real space) i0_real_error5.2270e+04
Rg (reciprocal space) rg_reciprocal20.83
I(0) (reciprocal space) i0_reciprocal5491000.0000
Solution quality estimate total_estimate0.6728
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.8
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha3.6470
Highest regularization parameter α highest_alpha760100.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 0.977; Sysdev: 0.000; Positv: 1.000; Valcen: 0.910; 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)