Research workbench
AlphaFold monomer V2.0 prediction for transcriptional activator protein trar (P33905)
Analyse AlphaFold monomer V2.0 prediction for transcriptional activator protein trar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P33905
- Type
- protein
- Length
- 234 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Transcriptional activator protein trar
- UniProt
- P33905
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional activator protein trar | protein | 234 | 54% helix, 15% strand | P33905 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.77 | 0.99 | 21 | empty |
| 2 | 182 | 0.55 | 0.80 | 20 | empty |
| 3 | 80 | 0.33 | 0.74 | 19 | empty |
Compared structures
- 1L3L · Crystal structure of a bacterial quorum-sensing transcription factor complexed with… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 1L3L · Crystal structure of a bacterial quorum-sensing transcription factor complexed with… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 1H0M · Three-dimensional structure of the quorum sensing protein trar bound to its autoinducer… · an experimental structure of the same protein · chain A against B, TM-score 0.94
- 1H0M · Three-dimensional structure of the quorum sensing protein TraR bound to its autoinducer… · an experimental structure of the same protein · chain A against B, TM-score 0.94
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 P33905
- Elsewhere: UniProt P33905 · AlphaFold DB P33905
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