Research workbench
AlphaFold monomer V2.0 prediction for oligosaccharides import ATP- binding protein msmx (P94360)
Analyse AlphaFold monomer V2.0 prediction for oligosaccharides import ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P94360
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Oligosaccharides import ATP-binding protein msmx
- UniProt
- P94360
- Pockets
- 1 · best druggability 0.56
Structure
1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligosaccharides import ATP-binding protein msmx | protein | 365 | 32% helix, 32% strand | P94360 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.56 | 0.80 | 25 | empty |
Compared structures
- 6YIR · Crystal structure of bacillus subtilis msmx ATPase · an experimental structure of the same protein · chain A against A, TM-score 0.92
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 P94360
- Elsewhere: UniProt P94360 · AlphaFold DB P94360
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