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Structure of an amyloid forming peptide klvffa from amyloid beta in complex with orange G

Analyse Structure of an amyloid forming peptide klvffa from amyloid beta in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OVJ
Type
protein
Length
24 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Klvffa hexapeptide segment from amyloid beta
UniProt
P05067
Ligands
ORA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 67% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DKlvffa hexapeptide segment from amyloid betaprotein60% helix, 67% strandP05067

Ligands and binding sites

  • ORA · 7-hydroxy-8-[(E)-phenyldiazenyl]naphthalene-1,3-disulfonic acid · ligand · 2 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

5 interfaces between chains.

  • A–B · 288 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 286 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 86 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 28 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 21 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3OVJ · Structure of an amyloid forming peptide KLVFFA from amyloid beta in complex with orange G · the same entry in another collection · chain D against D, 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 0.81

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