Research workbench
AlphaFold monomer V2.0 prediction for N-terminal acetyltransferase B complex auxiliary subunit NAA25 (F4KEY9)
Analyse AlphaFold monomer V2.0 prediction for N-terminal acetyltransferase B complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F4KEY9
- Type
- protein
- Length
- 1,065 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb31ae201d13A29F9351985f4eeF3179FD9486ab5
- Molecule
- N-terminal acetyltransferase B complex auxiliary subunit NAA25
- UniProt
- F4KEY9
- Pockets
- 14 · best druggability 0.84
Structure
1 distinct chain · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-terminal acetyltransferase B complex auxiliary subunit NAA25 | protein | 1065 | 71% helix, 1% strand | F4KEY9 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.84 | 0.85 | 96 | empty |
| 2 | 624 | 0.82 | 0.87 | 56 | empty |
| 3 | 623 | 0.81 | 0.86 | 60 | empty |
| 4 | 364 | 0.73 | 0.84 | 32 | empty |
| 5 | 190 | 0.68 | 0.86 | 24 | 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 F4KEY9
- Elsewhere: UniProt F4KEY9 · AlphaFold DB F4KEY9
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