Research workbench
AlphaFold monomer V2.0 prediction for glutathione import ATP-binding protein gsia (P75796)
Analyse AlphaFold monomer V2.0 prediction for glutathione import ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P75796
- Type
- protein
- Length
- 623 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Glutathione import ATP-binding protein gsia
- UniProt
- P75796
- Pockets
- 9 · best druggability 0.73
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione import ATP-binding protein gsia | protein | 623 | 37% helix, 25% strand | P75796 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 887 | 0.73 | 0.77 | 87 | empty |
| 2 | 84 | 0.71 | 0.95 | 23 | empty |
| 3 | 395 | 0.67 | 0.80 | 43 | empty |
| 4 | 170 | 0.52 | 0.78 | 18 | empty |
| 5 | 195 | 0.52 | 0.77 | 23 | empty |
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 P75796
- Elsewhere: UniProt P75796 · AlphaFold DB P75796
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