Research workbench
AlphaFold monomer V2.0 prediction for lps-assembly protein lptd (Q9KUR9)
Analyse AlphaFold monomer V2.0 prediction for lps-assembly protein lptd (Q9KUR9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9KUR9
- Type
- protein
- Length
- 783 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa772A41B3Ee4c395dFc35479410bf9cE5D840d7f
- Molecule
- Lps-assembly protein lptd
- UniProt
- Q9KUR9
- Pockets
- 6 · best druggability 0.79
Structure
1 distinct chain · 4% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lps-assembly protein lptd | protein | 783 | 4% helix, 56% strand | Q9KUR9 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 914 | 0.79 | 0.81 | 108 | empty |
| 2 | 788 | 0.76 | 0.80 | 69 | empty |
| 3 | 911 | 0.73 | 0.77 | 94 | empty |
| 4 | 288 | 0.59 | 0.79 | 34 | empty |
| 5 | 367 | 0.56 | 0.75 | 41 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q9KUR9
- Elsewhere: UniProt Q9KUR9 · AlphaFold DB Q9KUR9
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