Research workbench
AlphaFold monomer V2.0 prediction for TRNA(MET) cytidine acetate ligase (B7HMA5)
Analyse AlphaFold monomer V2.0 prediction for TRNA(MET) cytidine acetate ligase (B7HMA5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7HMA5
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- TRNA(MET) cytidine acetate ligase
- UniProt
- B7HMA5
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA(MET) cytidine acetate ligase | protein | 393 | 53% helix, 10% strand | B7HMA5 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 610 | 0.77 | 0.83 | 55 | empty |
| 2 | 250 | 0.67 | 0.84 | 31 | empty |
| 3 | 94 | 0.54 | 0.84 | 17 | empty |
| 4 | 68 | 0.32 | 0.75 | 18 | 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 B7HMA5
- Elsewhere: UniProt B7HMA5 · AlphaFold DB B7HMA5
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