Research workbench
AlphaFold monomer V2.0 prediction for H repeat-associated putative transposase yhhi (P28912)
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
- P28912
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- H repeat-associated putative transposase yhhi
- UniProt
- P28912
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H repeat-associated putative transposase yhhi | protein | 378 | 47% helix, 20% strand | P28912 |
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 | 79 | 0.65 | 0.92 | 18 | empty |
| 2 | 121 | 0.46 | 0.78 | 19 | empty |
| 3 | 100 | 0.45 | 0.79 | 20 | empty |
| 4 | 66 | 0.29 | 0.73 | 16 | 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 P28912
- Elsewhere: UniProt P28912 · AlphaFold DB P28912
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