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Metal binding domain of rat beta-amyloid

Analyse Metal binding domain of rat beta-amyloid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LI9
Type
protein
Length
32 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amyloid beta A4 protein
UniProt
P08592
Ligands
ACE, ZN, NH2

Structure

solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAmyloid beta A4 proteinprotein160% helix, 0% strandP08592

Ligands and binding sites

  • ACE · Acetyl group · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · chains A, B
  • NH2 · Amino group · ion · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 417 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 2LI9 · Metal binding domain of rat beta-amyloid · the same entry in another collection · chain A against A, TM-score 1.00
  • P08592 · AlphaFold monomer V2.0 prediction for amyloid-beta A4 protein (P08592) · a predicted model of the same protein · chain A against A, TM-score 0.20

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