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Structure of segment mvggvvia from the amyloid-beta peptide (ab, residues 35-42), alternate polymorph 2

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
2Y3L
Type
protein
Length
32 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amyloid beta A4 protein
UniProt
P05067

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 63% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, GAmyloid beta A4 proteinprotein80% helix, 63% strandP05067

Interfaces

6 interfaces between chains.

  • B–G · 304 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 300 Ų buried · 8 hydrogen bonds · protein-protein
  • C–G · 161 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 154 Ų buried · 0 hydrogen bonds · protein-protein
  • A–G · 112 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2Y3L · Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42)… · the same entry in another collection · chain G against G, 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 0.69

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