Research workbench
X-ray structure of amyloid beta PEPTIDE:ANTIBODY (ABETA1-40:12A11) complex
Analyse X-ray structure of amyloid beta PEPTIDE:ANTIBODY (ABETA1-40:12A11) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IFN
- Type
- protein
- Length
- 440 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 12A11 Fab antibody heavy chain; 12A11 Fab antibody light chain; Amyloid beta A4 protein
- UniProt
- P05067
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | 12A11 Fab antibody heavy chain | protein | 215 | 8% helix, 54% strand | — |
| L | 12A11 Fab antibody light chain | protein | 219 | 7% helix, 51% strand | — |
| P | Amyloid beta A4 protein | protein | 6 | 0% helix, 17% strand | P05067 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.51 | 0.74 | 44 | empty |
| 2 | 84 | 0.41 | 0.78 | 18 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1822 Ų buried · 20 hydrogen bonds · protein-protein
- L–P · 340 Ų buried · 9 hydrogen bonds · protein-protein
- H–P · 334 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3IFN · X-ray structure of amyloid beta peptide:antibody (Abeta1-40:12A11) 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 0.72
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 3IFN · PDBe 3IFN · UniProt P05067
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