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Solid-state mas NMR structure of the hellf prion amyloid fibrils

Analyse Solid-state mas NMR structure of the hellf prion amyloid fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EKA
Type: protein
Length: 265 residues
Chains: 5
Method: solid-state nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 2
UniProt: B2B1E9
Pockets: 1 · best druggability 0.61

Structure

solid-state nmr · 1 distinct chain · 8% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 2	protein	53	8% helix, 58% strand	B2B1E9

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	323	0.61	0.78	47	empty

Interfaces

4 interfaces between chains.

D–E · 1100 Å² buried · 33 hydrogen bonds · protein-protein
C–D · 1099 Å² buried · 34 hydrogen bonds · protein-protein
B–C · 1098 Å² buried · 33 hydrogen bonds · protein-protein
A–B · 1095 Å² buried · 33 hydrogen bonds · protein-protein

Compared structures

6EKA · Solid-state MAS NMR structure of the HELLF prion amyloid fibrils · the same entry in another collection · chain A against A, 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 B2B1E9
Elsewhere: RCSB PDB 6EKA · PDBe 6EKA · UniProt B2B1E9

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