Research workbench
AlphaFold monomer V2.0 prediction for putative ABC transporter ATP- binding protein MG187 homolog (P75264)
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
- P75264
- Type
- protein
- Length
- 586 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Putative ABC transporter ATP-binding protein MG187 homolog
- UniProt
- P75264
- Pockets
- 5 · best druggability 0.62
Structure
1 distinct chain · 53% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC transporter ATP-binding protein MG187 homolog | protein | 586 | 53% helix, 20% strand | P75264 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.62 | 0.77 | 42 | empty |
| 2 | 289 | 0.56 | 0.76 | 40 | empty |
| 3 | 99 | 0.43 | 0.78 | 20 | empty |
| 4 | 71 | 0.34 | 0.76 | 19 | empty |
| 5 | 91 | 0.32 | 0.73 | 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 P75264
- Elsewhere: UniProt P75264 · AlphaFold DB P75264
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