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MolNFT v1 · #176761 · protein

Cryo-EM structure of amyloid fibril formed by familial prion disease- related mutation E196K

7DWV · Major prion protein: “Cryo-EM structure of amyloid fibril formed by familial prion disease- related mutation E196K”. Electron microscopy, 4 pockets (best druggability 0.58). MolNFT v1 #176761 on GenesisL1: 3D structure, binding…

PDB
7DWV
Type
protein
Length
258 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major prion protein
UniProt
P04156
Pockets
4 · best druggability 0.58

Structure

electron microscopy · 1 distinct chain · 0% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FMajor prion proteinprotein430% helix, 16% strandP04156

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11890.580.8127empty
23190.540.7536empty
33010.530.7536empty
41470.500.7930empty

Interfaces

12 interfaces between chains.

  • D–E · 1840 Ų buried · 46 hydrogen bonds · protein-protein
  • B–C · 1838 Ų buried · 46 hydrogen bonds · protein-protein
  • E–F · 1837 Ų buried · 46 hydrogen bonds · protein-protein
  • A–B · 1834 Ų buried · 46 hydrogen bonds · protein-protein
  • B–D · 144 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 7DWV · Cryo-EM structure of amyloid fibril formed by familial prion disease-related mutation… · the same entry in another collection · chain A against A, TM-score 1.00

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