Research workbench
AlphaFold monomer V2.0 prediction for H repeat-associated putative transposase ydcc (P28917)
Analyse AlphaFold monomer V2.0 prediction for H repeat-associated putative transposase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28917
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAE6e7eC4cC5F9618Bc5ee759C76FD0817630792f
- Molecule
- H repeat-associated putative transposase ydcc
- UniProt
- P28917
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H repeat-associated putative transposase ydcc | protein | 378 | 46% helix, 20% strand | P28917 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.45 | 0.82 | 17 | empty |
| 2 | 107 | 0.41 | 0.77 | 21 | empty |
| 3 | 54 | 0.32 | 0.77 | 17 | empty |
| 4 | 55 | 0.25 | 0.72 | 17 | 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 P28917
- Elsewhere: UniProt P28917 · AlphaFold DB P28917
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