Research workbench
AlphaFold monomer V2.0 prediction for branched-chain-amino-acid aminotransferase atnh (Q5AV02)
Analyse AlphaFold monomer V2.0 prediction for branched-chain-amino-acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5AV02
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBb6f434FB4BD201f364930eace54164F9Da0c1ce
- Molecule
- Branched-chain-amino-acid aminotransferase atnh
- UniProt
- Q5AV02
- Pockets
- 3 · best druggability 0.63
Structure
1 distinct chain · 25% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Branched-chain-amino-acid aminotransferase atnh | protein | 396 | 25% helix, 29% strand | Q5AV02 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.63 | 0.79 | 41 | empty |
| 2 | 254 | 0.56 | 0.77 | 34 | empty |
| 3 | 72 | 0.47 | 0.83 | 16 | 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 Q5AV02
- Elsewhere: UniProt Q5AV02 · AlphaFold DB Q5AV02
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