Research workbench

Mouse prion protein (121-231) with mutations Y225A and Y226A

Analyse Mouse prion protein (121-231) with mutations Y225A and Y226A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KFM
Type: protein
Length: 113 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major prion protein
UniProt: P04925

Structure

solution nmr · 1 distinct chain · 50% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major prion protein	protein	113	50% helix, 4% strand	P04925

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2KFM · Mouse Prion Protein (121-231) with Mutations Y225A and Y226A · the same entry in another collection · chain A against A, TM-score 1.00
P04925 · AlphaFold monomer V2.0 prediction for major prion protein (P04925) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P04925
Elsewhere: RCSB PDB 2KFM · PDBe 2KFM · UniProt P04925

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