Research workbench
AlphaFold monomer V2.0 prediction for yop proteins translocation protein H (P68590)
Analyse AlphaFold monomer V2.0 prediction for yop proteins translocation protein H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P68590
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Yop proteins translocation protein H
- UniProt
- P68590
- Pockets
- 1 · best druggability 0.46
Structure
1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Yop proteins translocation protein H | protein | 165 | 63% helix, 0% strand | P68590 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.46 | 0.74 | 30 | empty |
Compared structures
- 1Z21 · Crystal structure of the core domain of Yersinia pestis virulence factor YopR · an experimental structure of the same protein · chain A against A, TM-score 0.58
- 1Z21 · Crystal structure of the core domain of yersinia pestis virulence factor yopr · an experimental structure of the same protein · chain A against A, TM-score 0.58
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 P68590
- Elsewhere: UniProt P68590 · AlphaFold DB P68590
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