Research workbench
AlphaFold monomer V2.0 prediction for prepilin leader PEPTIDASE/N-methyltransferase (O30387)
Analyse AlphaFold monomer V2.0 prediction for prepilin leader… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O30387
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe9087b4D2Dbe42150dd056Cf60524296F5E4c09F
- Molecule
- Prepilin leader PEPTIDASE/N-methyltransferase
- UniProt
- O30387
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 62% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prepilin leader PEPTIDASE/N-methyltransferase | protein | 335 | 62% helix, 2% strand | O30387 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.70 | 0.82 | 43 | empty |
| 2 | 300 | 0.64 | 0.81 | 36 | empty |
| 3 | 581 | 0.62 | 0.74 | 56 | empty |
| 4 | 77 | 0.36 | 0.76 | 14 | empty |
| 5 | 56 | 0.33 | 0.77 | 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 O30387
- Elsewhere: UniProt O30387 · AlphaFold DB O30387
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