Research workbench
X-ray structure of amyloid beta PEPTIDE:ANTIBODY (ABETA1-7:12A11) complex
Analyse X-ray structure of amyloid beta PEPTIDE:ANTIBODY (ABETA1-7:12A11) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IFL
- Type
- protein
- Length
- 439 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 12A11 Fab antibody light chain; 12A11 Fab antibody heavy chain; Amyloid beta A4 protein
- UniProt
- P05067
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | 12A11 Fab antibody light chain | protein | 218 | 6% helix, 51% strand | — |
| H | 12A11 Fab antibody heavy chain | protein | 214 | 6% helix, 55% strand | — |
| P | Amyloid beta A4 protein | protein | 7 | 0% helix, 14% strand | P05067 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.42 | 0.74 | 21 | empty |
| 2 | 69 | 0.37 | 0.78 | 16 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1797 Ų buried · 19 hydrogen bonds · protein-protein
- L–P · 334 Ų buried · 7 hydrogen bonds · protein-protein
- H–P · 322 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3IFL · X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12A11) complex · the same entry in another collection · chain L against L, TM-score 1.00
- P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain P against A, TM-score 0.54
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 3IFL · PDBe 3IFL · UniProt P05067
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.