Research workbench
AlphaFold monomer V2.0 prediction for putative ABC transporter ATP- binding protein MM_1037 (Q8PY27)
Analyse AlphaFold monomer V2.0 prediction for putative ABC transporter ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8PY27
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbF8467B100eddcD57b40BcA629dAe7126b34CBf1
- Molecule
- Putative ABC transporter ATP-binding protein MM_1037
- UniProt
- Q8PY27
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC transporter ATP-binding protein MM_1037 | protein | 274 | 45% helix, 21% strand | Q8PY27 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.60 | 0.79 | 26 | empty |
| 2 | 152 | 0.49 | 0.78 | 28 | empty |
| 3 | 64 | 0.45 | 0.83 | 13 | empty |
| 4 | 57 | 0.37 | 0.79 | 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 Q8PY27
- Elsewhere: UniProt Q8PY27 · AlphaFold DB Q8PY27
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