Research workbench
A partially folded structure of amyloid-BETA(1 40) in an aqueous environment
Analyse A partially folded structure of amyloid-BETA(1 40) in an aqueous environment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LFM
- Type
- protein
- Length
- 40 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-amyloid protein 40
- UniProt
- P05067
Structure
solution nmr · 1 distinct chain · 25% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-amyloid protein 40 | protein | 40 | 25% helix, 0% strand | P05067 |
Compared structures
- 2LFM · A partially folded structure of amyloid-beta(1 40) in an aqueous environment · the same entry in another collection · chain A against A, 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 0.36
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 2LFM · PDBe 2LFM · UniProt P05067
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