4bxl

Structure of alpha-synuclein in complex with an engineered binding protein

Method: SOLUTION NMR Dmax: 48.0 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 35–56 Fragment:RESIDUES 35-56 AS69 × 2 SOLUTION NMR NMR measurement conditions:pH 7.4;303 K;Ionic strength (raw mmCIF value) 0.07;Pressure 1.0 NMR measurement conditions:pH 7.4;303 K;Ionic strength (raw mmCIF value) 0.07;Pressure 1.0 NMR sample composition:93% H2O/7% D2O NMR sample composition:93% H2O/7% D2O Resolution not provided

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–22; UniProt 35–56

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 4bxl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4bxl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4bxl
Deposition date deposition_date2013-07-12
Structure title titleStructure of alpha-synuclein in complex with an engineered binding protein
Keywords keywords;FIBRIL, AMYLOID, PARKINSON'S DISEASE, PROTEIN AGGREGATION, PROTEIN ENGINEERING, PROTEIN MISFOLDING, SCAFFOLD PROTEINS ;; FIBRIL
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.84
Radius of gyration Rg (electron density) rg_electron13.23
Forward intensity I(0) i0222750000.00
Molecular weight molecular_weight123600.0 kDa
Excluded volume excluded_volume153720 ų
Envelope volume envelope_volume21040 ų
Hydration-shell volume shell_volume12528 ų
Envelope diameter envelope_diameter52.3
Shell Rg shell_rg20.04
Envelope Rg envelope_rg14.71
Shape Rg shape_rg13.19
Total Rg total_rg13.57
Total atoms total_atoms17130
Residues n_residues1140
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 dmax48.0
Rg (real space) rg_real13.74
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.2280e+08
I(0) uncertainty (real space) i0_real_error2.7650e+06
Rg (reciprocal space) rg_reciprocal13.75
I(0) (reciprocal space) i0_reciprocal222800000.0000
Solution quality estimate total_estimate0.8470
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.053
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha198100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4bxlA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id4bxlB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C

8. Citations (1)

9. Files and Curves (10)