Research workbench
Crystal structure of human frataxin variant W155F
Analyse Crystal structure of human frataxin variant W155F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S5F
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frataxin, mitochondrial
- EC
- 1.16.3.1
- UniProt
- Q16595
- Ligands
- MG
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frataxin, mitochondrial (EC 1.16.3.1) | protein | 120 | 29% helix, 28% strand | Q16595 |
| B | Frataxin, mitochondrial (EC 1.16.3.1) | protein | 125 | 34% helix, 26% strand | Q16595 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.33 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 888 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 3S5F · PDBe 3S5F · UniProt Q16595
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.