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Human prion protein variant V129 domain swapped dimer

Analyse Human prion protein variant V129 domain swapped dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HJ5
Type: protein
Length: 203 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major prion protein
UniProt: P04156

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major prion protein	protein	101	58% helix, 7% strand	P04156
B	Major prion protein	protein	102	58% helix, 7% strand	P04156

Interfaces

1 interface between chains.

A–B · 3273 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3HJ5 · Human prion protein variant V129 domain swapped dimer · 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 0.64

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 3HJ5 · PDBe 3HJ5 · UniProt P04156

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