MolNFT v1 · #180826 · protein

Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140

7LC9: “Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140”. Electron microscopy, 1 pocket (best druggability 0.61). MolNFT v1 #180826 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LC9
Type: protein
Length: 525 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-synuclein
UniProt: P37840
Pockets: 1 · best druggability 0.61

Structure

electron microscopy · 3 distinct chains · 0% helix, 70% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F, H, I, J, K	Alpha-synuclein	protein	38	0% helix, 74% strand	P37840
A, B, C, D, E, G	Alpha-synuclein	protein	51	0% helix, 63% strand	P37840
L	Alpha-synuclein	protein	29	0% helix, 79% strand	P37840

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.61	0.90	27	empty

Interfaces

37 interfaces between chains.

B–C · 2095 Å² buried · 63 hydrogen bonds · protein-protein
C–D · 2085 Å² buried · 70 hydrogen bonds · protein-protein
A–B · 2084 Å² buried · 64 hydrogen bonds · protein-protein
D–E · 2075 Å² buried · 67 hydrogen bonds · protein-protein
E–G · 2069 Å² buried · 58 hydrogen bonds · protein-protein

Compared structures

7LC9 · Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140 · the same entry in another collection · chain J against J, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P37840
Elsewhere: RCSB PDB 7LC9 · PDBe 7LC9 · UniProt P37840

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