Research workbench
AlphaFold monomer V2.0 prediction for N-terminal acetyltransferase B complex subunit NAA25 homolog (Q21986)
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
- Q21986
- Type
- protein
- Length
- 958 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- N-terminal acetyltransferase B complex subunit NAA25 homolog
- UniProt
- Q21986
- Pockets
- 12 · best druggability 0.62
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-terminal acetyltransferase B complex subunit NAA25 homolog | protein | 958 | 75% helix, 0% strand | Q21986 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.62 | 0.76 | 39 | empty |
| 2 | 216 | 0.57 | 0.79 | 23 | empty |
| 3 | 109 | 0.55 | 0.83 | 21 | empty |
| 4 | 136 | 0.54 | 0.81 | 18 | empty |
| 5 | 50 | 0.47 | 0.85 | 13 | 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 Q21986
- Elsewhere: UniProt Q21986 · AlphaFold DB Q21986
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