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

Analyse Structure of alpha-synuclein in complex with an engineered binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BXL
Type
protein
Length
114 residues
Chains
3
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
AS69; Alpha synuclein
UniProt
P37840
Pockets
1 · best druggability 0.35

Structure

solution nmr · 2 distinct chains · 41% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAS69protein4661% helix, 9% strand—
CAlpha synucleinprotein220% helix, 68% strandP37840

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.350.7718empty

Interfaces

3 interfaces between chains.

  • B–C · 665 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 643 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 398 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4BXL · Structure of alpha-synuclein in complex with an engineered binding protein · the same entry in another collection · chain A against A, TM-score 1.00

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