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AlphaFold monomer V2.0 prediction for acetyl-coenzyme a transferase nodx (A0A2I6PIZ1)
Analyse AlphaFold monomer V2.0 prediction for acetyl-coenzyme a transferase nodx… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A2I6PIZ1
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Acetyl-coenzyme a transferase nodx
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-coenzyme a transferase nodx | protein | 593 | 41% helix, 15% strand | — |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.76 | 0.83 | 53 | empty |
| 2 | 353 | 0.69 | 0.82 | 47 | empty |
| 3 | 55 | 0.39 | 0.81 | 14 | empty |
| 4 | 105 | 0.36 | 0.74 | 18 | empty |
| 5 | 50 | 0.36 | 0.80 | 18 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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