Research workbench
AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A7INL1)
Analyse AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A7INL1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7INL1
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Phosphate acyltransferase
- UniProt
- A7INL1
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acyltransferase | protein | 356 | 47% helix, 17% strand | A7INL1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.68 | 0.78 | 59 | empty |
| 2 | 134 | 0.44 | 0.76 | 17 | empty |
| 3 | 66 | 0.34 | 0.76 | 17 | empty |
| 4 | 82 | 0.30 | 0.72 | 16 | 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 A7INL1
- Elsewhere: UniProt A7INL1 · AlphaFold DB A7INL1
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