MolNFT v1 · #182809 · protein
Structure of ATATM3 in the inward-facing conformation with gssg bound
7N59 · ABC transporter B family member 25, mitochondrial: “Structure of ATATM3 in the inward-facing conformation with gssg bound”. Electron microscopy, 1 ligand (GDS), 20 pockets (best druggability 0.78). MolNFT v1 #182809 on GenesisL1: 3D…
- PDB
- 7N59
- Type
- protein
- Length
- 1,180 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter B family member 25, mitochondrial
- UniProt
- Q9LVM1
- Ligands
- GDS
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ABC transporter B family member 25, mitochondrial | protein | 590 | 62% helix, 9% strand | Q9LVM1 |
Ligands and binding sites
- GDS · Oxidized glutathione disulfide · ligand · chains A, 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 | 156 | 0.78 | 0.95 | 23 | empty |
| 2 | 554 | 0.74 | 0.82 | 48 | empty |
| 3 | 520 | 0.73 | 0.82 | 46 | empty |
| 4 | 293 | 0.70 | 0.84 | 43 | empty |
| 5 | 218 | 0.64 | 0.83 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 5707 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 7N59 · Structure of AtAtm3 in the inward-facing conformation with GSSG bound · the same entry in another collection · chain B against B, TM-score 1.00
- Q9LVM1 · AlphaFold monomer V2.0 prediction for ABC transporter B family member 25, mitochondrial… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q9LVM1
- Elsewhere: RCSB PDB 7N59 · PDBe 7N59 · UniProt Q9LVM1
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