Research workbench
AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 16, nata auxiliary subunit (Q9DBB4)
Analyse AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 16, nata… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9DBB4
- Type
- protein
- Length
- 864 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- N-alpha-acetyltransferase 16, nata auxiliary subunit
- UniProt
- Q9DBB4
- Pockets
- 13 · best druggability 0.67
Structure
1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase 16, nata auxiliary subunit | protein | 864 | 73% helix, 0% strand | Q9DBB4 |
Pockets
13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 679 | 0.67 | 0.76 | 42 | empty |
| 2 | 730 | 0.65 | 0.74 | 64 | empty |
| 3 | 273 | 0.54 | 0.76 | 31 | empty |
| 4 | 65 | 0.45 | 0.82 | 14 | empty |
| 5 | 86 | 0.43 | 0.79 | 15 | 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 Q9DBB4
- Elsewhere: UniProt Q9DBB4 · AlphaFold DB Q9DBB4
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