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Solution NMR structure of the V209M variant of the human prion protein (residues 90-231)

Analyse Solution NMR structure of the V209M variant of the human prion protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2M8T
Type: protein
Length: 112 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major prion protein
UniProt: P04156
Pockets: 3 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 49% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major prion protein	protein	112	49% helix, 4% strand	P04156

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.43	0.78	19	empty
2	61	0.32	0.76	13	empty
3	56	0.27	0.73	14	empty

Compared structures

2M8T · Solution NMR structure of the V209M variant of the human prion protein (residues 90-231) · the same entry in another collection · chain A against A, TM-score 1.00
P04156 · AlphaFold monomer V2.0 prediction for major prion protein (P04156) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 2M8T · PDBe 2M8T · UniProt P04156

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