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Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1

Analyse Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y3K
Type: protein
Length: 64 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Molecule: Amyloid beta A4 protein
UniProt: P05067

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 0% helix, 75% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Amyloid beta A4 protein	protein	8	0% helix, 75% strand	P05067

Interfaces

17 interfaces between chains.

A–B · 317 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 299 Å² buried · 9 hydrogen bonds · protein-protein
G–H · 299 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 297 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 178 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2Y3K · Structure of segment mvggvvia from the amyloid-beta peptide (ab, residues 35-42)… · the same entry in another collection · chain H against H, TM-score 1.00
P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain A against A, TM-score 0.67

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 2Y3K · PDBe 2Y3K · UniProt P05067

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