9e8w

Complex fibril structure of MSA alpha-synuclein with CNS-11g at 6 hours

Method: ELECTRON MICROSCOPY Dmax: 103.7 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 A1BGB 2-(4-benzyl-1-oxophthalazin-2(1H)-yl)-N-(2,6-dimethylphenyl)acetamide × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;30mM Tris-HCl, pH 7.4, with 1% DMSO cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 9e8w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e8w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e8w
Deposition date deposition_date2024-11-06
Structure title titleComplex fibril structure of MSA alpha-synuclein with CNS-11g at 6 hours
Keywords keywordsComplex structure of alpha-synuclein type I with small molecule CNS11G incubated for 6 hours., STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.92
Radius of gyration Rg (electron density) rg_electron32.55
Forward intensity I(0) i0212857000.00
Molecular weight molecular_weight76946.0 kDa
Excluded volume excluded_volume73806 ų
Envelope volume envelope_volume134840 ų
Hydration-shell volume shell_volume35228 ų
Envelope diameter envelope_diameter104.1
Shell Rg shell_rg38.60
Envelope Rg envelope_rg32.39
Shape Rg shape_rg32.54
Total Rg total_rg32.93
Total atoms total_atoms5850
Residues n_residues825
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 dmax103.7
Rg (real space) rg_real32.94
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real2.1290e+08
I(0) uncertainty (real space) i0_real_error3.6650e+06
Rg (reciprocal space) rg_reciprocal32.94
I(0) (reciprocal space) i0_reciprocal212900000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17950000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.812

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)