Research workbench
AlphaFold monomer V2.0 prediction for amino-acid acetyltransferase, mitochondrial (B2B2C5)
Analyse AlphaFold monomer V2.0 prediction for amino-acid acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2B2C5
- Type
- protein
- Length
- 674 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x75B24D2B0e9632594da11Dd7fB5CA6a718195Fd6
- Molecule
- Amino-acid acetyltransferase, mitochondrial
- UniProt
- B2B2C5
- Pockets
- 13 · best druggability 0.80
Structure
1 distinct chain · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amino-acid acetyltransferase, mitochondrial | protein | 674 | 36% helix, 15% strand | B2B2C5 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 730 | 0.80 | 0.84 | 86 | empty |
| 2 | 454 | 0.68 | 0.80 | 45 | empty |
| 3 | 153 | 0.65 | 0.86 | 26 | empty |
| 4 | 364 | 0.65 | 0.80 | 47 | empty |
| 5 | 150 | 0.61 | 0.84 | 27 | 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 B2B2C5
- Elsewhere: UniProt B2B2C5 · AlphaFold DB B2B2C5
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