Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Amyloid beta A4 protein | protein | 16 | 0% helix, 0% strand | P08592 |
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
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 P08592
- Elsewhere: RCSB PDB 2LI9 · PDBe 2LI9 · UniProt P08592
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