9v7c

The cryo-EM structure of FD4_orientation2 bound Lewy fold fibril.

Method: ELECTRON MICROSCOPY Dmax: 93.4 Å Quality: EXCELLENT

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain c; UniProt 32–101 Chain d; UniProt 32–101 Chain e; UniProt 32–101 Chain f; UniProt 32–101 Chain g; UniProt 32–101 Chain h; UniProt 32–101 Chain i; UniProt 32–101 Chain j; UniProt 32–101 Chain k; UniProt 32–101 Chain o; UniProt 32–101 Chain p; UniProt 32–101 Chain q; UniProt 32–101 Chain r; UniProt 32–101 Chain s; UniProt 32–101 Chain t; UniProt 32–101 Not recorded (2~{R})-1-fluoranyl-3-[[2-[(~{E})-2-[5-[6-(methylamino)pyridin-3-yl]pyridin-2-yl]ethenyl]-1,3-benzothiazol-6-yl]oxy]propan-2-ol × 18 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.30 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 c; PDBConstruct 1–69; UniProt 32–101 Author chain d; PDBConstruct 1–69; UniProt 32–101 Author chain e; PDBConstruct 1–69; UniProt 32–101 Author chain f; PDBConstruct 1–69; UniProt 32–101 Author chain g; PDBConstruct 1–69; UniProt 32–101 Author chain h; PDBConstruct 1–69; UniProt 32–101 Author chain i; PDBConstruct 1–69; UniProt 32–101 Author chain j; PDBConstruct 1–69; UniProt 32–101 Author chain k; PDBConstruct 1–69; UniProt 32–101 Author chain o; PDBConstruct 1–69; UniProt 32–101 Author chain p; PDBConstruct 1–69; UniProt 32–101 Author chain q; PDBConstruct 1–69; UniProt 32–101 Author chain r; PDBConstruct 1–69; UniProt 32–101 Author chain s; PDBConstruct 1–69; UniProt 32–101 Author chain t; PDBConstruct 1–69; UniProt 32–101

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 9v7c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v7c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v7c
Deposition date deposition_date2025-05-27
Structure title titleThe cryo-EM structure of FD4_orientation2 bound Lewy fold fibril.
Keywords keywordsamyloid, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.13
Radius of gyration Rg (electron density) rg_electron29.37
Forward intensity I(0) i0369919000.00
Molecular weight molecular_weight102450.0 kDa
Excluded volume excluded_volume98814 ų
Envelope volume envelope_volume171490 ų
Hydration-shell volume shell_volume46490 ų
Envelope diameter envelope_diameter98.1
Shell Rg shell_rg38.52
Envelope Rg envelope_rg29.50
Shape Rg shape_rg29.34
Total Rg total_rg30.00
Total atoms total_atoms7773
Residues n_residues1035
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 dmax93.4
Rg (real space) rg_real29.98
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real3.6990e+08
I(0) uncertainty (real space) i0_real_error5.4640e+06
Rg (reciprocal space) rg_reciprocal30.05
I(0) (reciprocal space) i0_reciprocal369900000.0000
Solution quality estimate total_estimate0.9035
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89200000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)