8zlo

F0502B-bound E46K alpha-synuclein fibril

Method: ELECTRON MICROSCOPY Dmax: 98.9 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 × 12 PDB declaration: 12-meric(12) 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 Chain G; UniProt 45–99 Chain H; UniProt 45–99 Chain I; UniProt 45–99 Chain J; UniProt 45–99 Chain O; UniProt 45–99 Chain T; UniProt 45–99 Not recorded 1KI 2-bromanyl-4-[(~{E})-2-[6-[2-(2-fluoranylethoxy)ethyl-methyl-amino]-5-methyl-1,3-benzothiazol-2-yl]ethenyl]phenol × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 Author chain G; PDBConstruct 1–55; UniProt 45–99 Author chain H; PDBConstruct 1–55; UniProt 45–99 Author chain I; PDBConstruct 1–55; UniProt 45–99 Author chain J; PDBConstruct 1–55; UniProt 45–99 Author chain O; PDBConstruct 1–55; UniProt 45–99 Author chain T; 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 8zlo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zlo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zlo
Deposition date deposition_date2024-05-20
最后修订 last_revision2024-09-11
Structure title titleF0502B-bound E46K alpha-synuclein fibril
Keywords keywordsamyloid fibril, complex, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.13
Radius of gyration Rg (electron density) rg_electron27.80
Forward intensity I(0) i076504600.00
Molecular weight molecular_weight69216.0 kDa
Excluded volume excluded_volume86963 ų
Envelope volume envelope_volume103420 ų
Hydration-shell volume shell_volume31776 ų
Envelope diameter envelope_diameter104.0
Shell Rg shell_rg34.56
Envelope Rg envelope_rg28.31
Shape Rg shape_rg27.70
Total Rg total_rg28.78
Total atoms total_atoms4816
Residues n_residues660
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 dmax98.9
Rg (real space) rg_real28.28
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real7.6500e+07
I(0) uncertainty (real space) i0_real_error1.2360e+06
Rg (reciprocal space) rg_reciprocal28.24
I(0) (reciprocal space) i0_reciprocal76500000.0000
Solution quality estimate total_estimate0.8470
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.2
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis-0.210
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43600000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.852; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)