Research workbench
AlphaFold monomer V2.0 prediction for methionine import ATP-binding protein metn (Q5X484)
Analyse AlphaFold monomer V2.0 prediction for methionine import ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5X484
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Methionine import ATP-binding protein metn
- UniProt
- Q5X484
- Pockets
- 2 · best druggability 0.55
Structure
1 distinct chain · 40% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine import ATP-binding protein metn | protein | 341 | 40% helix, 30% strand | Q5X484 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.55 | 0.78 | 22 | empty |
| 2 | 50 | 0.34 | 0.78 | 12 | 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 Q5X484
- Elsewhere: UniProt Q5X484 · AlphaFold DB Q5X484
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