Research workbench
The solution structure of the the C-terminal domain of frataxin, the protein responsible for friedreich ataxia
Analyse The solution structure of the the C-terminal domain of frataxin, the protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LY7
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frataxin
- UniProt
- Q16595
Structure
solution nmr · 1 distinct chain · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frataxin | protein | 121 | 26% helix, 26% strand | Q16595 |
Compared structures
- 1LY7 · The solution structure of the the c-terminal domain of frataxin, the protein responsible… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16595 · AlphaFold monomer V2.0 prediction for frataxin, mitochondrial (Q16595) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q16595
- Elsewhere: RCSB PDB 1LY7 · PDBe 1LY7 · UniProt Q16595
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