Research workbench
AlphaFold monomer V2.0 prediction for translocase of chloroplast 108, chloroplastic (A9SY65)
Analyse AlphaFold monomer V2.0 prediction for translocase of chloroplast 108… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9SY65
- Type
- protein
- Length
- 994 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Translocase of chloroplast 108, chloroplastic
- UniProt
- A9SY65
- Pockets
- 11 · best druggability 0.69
Structure
1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translocase of chloroplast 108, chloroplastic | protein | 994 | 29% helix, 21% strand | A9SY65 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.69 | 0.79 | 61 | empty |
| 2 | 545 | 0.63 | 0.75 | 49 | empty |
| 3 | 52 | 0.57 | 0.91 | 15 | empty |
| 4 | 190 | 0.52 | 0.78 | 35 | empty |
| 5 | 192 | 0.49 | 0.76 | 31 | 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 A9SY65
- Elsewhere: UniProt A9SY65 · AlphaFold DB A9SY65
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