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Structure of type II prion filaments from gerstmann-straussler- scheinker disease

Analyse Structure of type II prion filaments from gerstmann-straussler- scheinker… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UN5
Type: protein
Length: 620 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major prion protein
UniProt: P04156
Pockets: 3 · best druggability 0.72

Structure

electron microscopy · 1 distinct chain · 0% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, B, C, D, H, F, G, I, J	Major prion protein	protein	62	0% helix, 42% strand	P04156

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1057	0.72	0.76	86	empty
2	1133	0.72	0.76	84	empty
3	113	0.31	0.72	32	empty

Interfaces

23 interfaces between chains.

E–B · 2401 Å² buried · 62 hydrogen bonds · protein-protein
E–C · 2391 Å² buried · 60 hydrogen bonds · protein-protein
A–B · 2388 Å² buried · 60 hydrogen bonds · protein-protein
G–I · 2377 Å² buried · 67 hydrogen bonds · protein-protein
H–I · 2376 Å² buried · 63 hydrogen bonds · protein-protein

Compared structures

7UN5 · Structure of Type II Prion filaments from Gerstmann-Straussler-Scheinker disease · the same entry in another collection · chain E against E, 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 P04156
Elsewhere: RCSB PDB 7UN5 · PDBe 7UN5 · UniProt P04156

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