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Cryoem tetra protofilament structure of the hamster prion 108-144 fibril

Analyse Cryoem tetra protofilament structure of the hamster prion 108-144 fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7YAT
Type
protein
Length
600 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major prion protein
UniProt
P04273
Pockets
12 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 0% helix, 60% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, X, YMajor prion proteinprotein250% helix, 60% strandP04273

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12830.800.9147empty
22790.790.9047empty
32810.780.9046empty
42790.780.8948empty
5780.670.9224empty

Interfaces

64 interfaces between chains.

  • B–C · 986 Ų buried · 38 hydrogen bonds · protein-protein
  • S–Y · 983 Ų buried · 35 hydrogen bonds · protein-protein
  • T–U · 981 Ų buried · 33 hydrogen bonds · protein-protein
  • M–R · 975 Ų buried · 33 hydrogen bonds · protein-protein
  • A–F · 965 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 7YAT · CryoEM tetra protofilament structure of the hamster prion 108-144 fibril · the same entry in another collection · chain A against A, TM-score 1.00

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