Research workbench
AlphaFold monomer V2.0 prediction for protein tic 100 (Q8LPR8)
Analyse AlphaFold monomer V2.0 prediction for protein tic 100 (Q8LPR8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8LPR8
- Type
- protein
- Length
- 871 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x98c95d7EC463682453dDA6620Db0cecEae0560fA
- Molecule
- Protein tic 100
- UniProt
- Q8LPR8
- Pockets
- 7 · best druggability 0.66
Structure
1 distinct chain · 28% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tic 100 | protein | 871 | 28% helix, 12% strand | Q8LPR8 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.66 | 0.76 | 48 | empty |
| 2 | 516 | 0.61 | 0.74 | 46 | empty |
| 3 | 277 | 0.52 | 0.75 | 30 | empty |
| 4 | 153 | 0.43 | 0.74 | 27 | empty |
| 5 | 126 | 0.40 | 0.74 | 23 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 8Z9Y · Cryo-EM Structure of the Arabidopsis thaliana TIC Complex · an experimental structure of the same protein · chain A against D, TM-score 0.28
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 Q8LPR8
- Elsewhere: UniProt Q8LPR8 · AlphaFold DB Q8LPR8
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