Research workbench
AlphaFold monomer V2.0 prediction for putative hth-type transcriptional regulatory protein M1425_1284 (C3MYR0)
Analyse AlphaFold monomer V2.0 prediction for putative hth-type transcriptional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3MYR0
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7D876F364ae377f396cf395997491B94DB9a3335
- Molecule
- Putative hth-type transcriptional regulatory protein M1425_1284
- UniProt
- C3MYR0
- Pockets
- 3 · best druggability 0.46
Structure
1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative hth-type transcriptional regulatory protein M1425_1284 | protein | 310 | 42% helix, 20% strand | C3MYR0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.46 | 0.77 | 23 | empty |
| 2 | 151 | 0.44 | 0.75 | 27 | empty |
| 3 | 81 | 0.32 | 0.74 | 20 | 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 C3MYR0
- Elsewhere: UniProt C3MYR0 · AlphaFold DB C3MYR0
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