Research workbench

Amyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutation

Analyse Amyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O4J
Type: protein
Length: 22 residues
Chains: 2
Method: electron crystallography
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.402
Molecule: Amyloid-beta precursor protein
UniProt: P05067

Structure

electron crystallography · resolution 1.402 · 1 distinct chain · 0% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amyloid-beta precursor protein	protein	11	0% helix, 36% strand	P05067

Interfaces

1 interface between chains.

A–B · 306 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6O4J · Amyloid beta klvffaenvgs 16-26 D23N iowa mutation · the same entry in another collection · chain A against A, TM-score 1.00
P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain B against A, TM-score 0.41

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 P05067
Elsewhere: RCSB PDB 6O4J · PDBe 6O4J · UniProt P05067

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