MolNFT v1 · #100468 · protein
Structure of the glutathione bound mitochondrial ABC transporter, ATM1
4MYH · Iron-sulfur clusters transporter ATM1, mitochondrial: “Structure of the glutathione bound mitochondrial ABC transporter, ATM1”. X-ray diffraction, 1 ligand (GSH), 20 pockets (best druggability 0.84). MolNFT v1 #100468 on GenesisL1…
- PDB
- 4MYH
- Type
- protein
- Length
- 1,794 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron-sulfur clusters transporter ATM1, mitochondrial
- EC
- 3.6.3.44
- UniProt
- P40416
- Ligands
- GSH
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | Iron-sulfur clusters transporter ATM1, mitochondrial (EC 3.6.3.44) | protein | 598 | 61% helix, 10% strand | P40416 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.84 | 0.85 | 76 | empty |
| 2 | 216 | 0.66 | 0.84 | 39 | empty |
| 3 | 234 | 0.64 | 0.82 | 38 | empty |
| 4 | 122 | 0.57 | 0.84 | 25 | empty |
| 5 | 121 | 0.56 | 0.83 | 27 | empty |
Interfaces
2 interfaces between chains.
- A–B · 7020 Ų buried · 49 hydrogen bonds · protein-protein
- C–B · 472 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4MYH · Structure of the Glutathione bound mitochondrial ABC transporter, Atm1 · the same entry in another collection · chain A against A, TM-score 1.00
- P40416 · AlphaFold monomer V2.0 prediction for iron-sulfur clusters transporter ATM1… · a predicted model of the same protein · chain C against A, TM-score 0.97
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 P40416
- Elsewhere: RCSB PDB 4MYH · PDBe 4MYH · UniProt P40416
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