Research workbench
1.38 a structure of human frataxin variant Q148G
Analyse 1.38 a structure of human frataxin variant Q148G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T3T
- Type
- protein
- Length
- 480 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frataxin, mitochondrial
- EC
- 1.16.3.1
- UniProt
- Q16595
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Frataxin, mitochondrial (EC 1.16.3.1) | protein | 120 | 33% helix, 28% strand | Q16595 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 300 | 0.60 | 0.78 | 33 | empty |
| 2 | 72 | 0.48 | 0.83 | 18 | empty |
| 3 | 156 | 0.39 | 0.73 | 19 | empty |
| 4 | 72 | 0.39 | 0.79 | 21 | empty |
| 5 | 86 | 0.38 | 0.77 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–B · 644 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 160 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 154 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 99 Ų buried · 0 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 3T3T · PDBe 3T3T · UniProt Q16595
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