Research workbench
AlphaFold monomer V2.0 prediction for erythromycin resistance ATP- binding protein msra (P23212)
Analyse AlphaFold monomer V2.0 prediction for erythromycin resistance ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23212
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Erythromycin resistance ATP-binding protein msra
- UniProt
- P23212
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin resistance ATP-binding protein msra | protein | 488 | 42% helix, 23% strand | P23212 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.73 | 0.80 | 71 | empty |
| 2 | 331 | 0.62 | 0.79 | 52 | empty |
| 3 | 68 | 0.38 | 0.79 | 16 | empty |
| 4 | 55 | 0.30 | 0.75 | 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 P23212
- Elsewhere: UniProt P23212 · AlphaFold DB P23212
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