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Crystal structure of human frataxin variant W155R, one of the FRIEDREICH'S ataxia point mutations
Analyse Crystal structure of human frataxin variant W155R, one of the FRIEDREICH'S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S5E
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frataxin, mitochondrial
- EC
- 1.16.3.1
- UniProt
- Q16595
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frataxin, mitochondrial (EC 1.16.3.1) | protein | 121 | 29% helix, 27% strand | Q16595 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3S5E · Crystal structure of human frataxin variant W155R, one of the Friedreich's ataxia point… · 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 0.99
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 3S5E · PDBe 3S5E · UniProt Q16595
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