7yns

SIL5-bound alpha-synuclein fibrils

Method: ELECTRON MICROSCOPY Dmax: 96.0 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 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 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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

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 7yns

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7yns
Deposition date deposition_date2022-07-31
Structure title titleSIL5-bound alpha-synuclein fibrils
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_guinier26.87
Radius of gyration Rg (electron density) rg_electron27.32
Forward intensity I(0) i020680400.00
Molecular weight molecular_weight35916.0 kDa
Excluded volume excluded_volume45706 ų
Envelope volume envelope_volume59759 ų
Hydration-shell volume shell_volume19839 ų
Envelope diameter envelope_diameter99.2
Shell Rg shell_rg31.69
Envelope Rg envelope_rg27.76
Shape Rg shape_rg27.31
Total Rg total_rg27.89
Total atoms total_atoms2526
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 dmax96.0
Rg (real space) rg_real27.02
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real2.0680e+07
I(0) uncertainty (real space) i0_real_error3.4010e+05
Rg (reciprocal space) rg_reciprocal26.98
I(0) (reciprocal space) i0_reciprocal20680000.0000
Solution quality estimate total_estimate0.8540
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.373
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1213000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.668; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)