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MolNFT v1 · #155928 · protein

Cryo-EM structure of amyloid fibril formed by full-length human prion protein

6LNI · Major prion protein: “Cryo-EM structure of amyloid fibril formed by full-length human prion protein”. Electron microscopy, 3 pockets (best druggability 0.77). MolNFT v1 #155928 on GenesisL1: 3D structure, binding sites and pockets…

PDB
6LNI
Type
protein
Length
600 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major prion protein
UniProt
P04156
Pockets
3 · best druggability 0.77

Structure

electron microscopy · 1 distinct chain · 0% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JMajor prion proteinprotein600% helix, 50% strandP04156

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13870.770.8630empty
22340.720.8734empty
32270.710.8734empty

Interfaces

17 interfaces between chains.

  • H–I · 2691 Ų buried · 75 hydrogen bonds · protein-protein
  • C–D · 2685 Ų buried · 75 hydrogen bonds · protein-protein
  • B–C · 2675 Ų buried · 71 hydrogen bonds · protein-protein
  • I–J · 2675 Ų buried · 70 hydrogen bonds · protein-protein
  • G–H · 2674 Ų buried · 72 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 6LNI · Cryo-EM structure of amyloid fibril formed by full-length human prion protein · the same entry in another collection · chain A against A, TM-score 1.00

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