Research workbench
AlphaFold monomer V2.0 prediction for probable transcriptional regulatory protein BAMEG_4045 (C3LH91)
Analyse AlphaFold monomer V2.0 prediction for probable transcriptional regulatory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3LH91
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Probable transcriptional regulatory protein BAMEG_4045
- UniProt
- C3LH91
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 48% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable transcriptional regulatory protein BAMEG_4045 | protein | 239 | 48% helix, 23% strand | C3LH91 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.71 | 0.88 | 24 | empty |
| 2 | 65 | 0.67 | 0.95 | 17 | empty |
| 3 | 225 | 0.55 | 0.78 | 25 | empty |
| 4 | 52 | 0.27 | 0.74 | 15 | 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 C3LH91
- Elsewhere: UniProt C3LH91 · AlphaFold DB C3LH91
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