Research workbench
AlphaFold monomer V2.0 prediction for transcription TERMINATION/ANTITERMINATION protein nusa (P32727)
Analyse AlphaFold monomer V2.0 prediction for transcription TERMINATION/ANTITERMINATION… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P32727
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Transcription TERMINATION/ANTITERMINATION protein nusa
- UniProt
- P32727
- Pockets
- 2 · best druggability 0.31
Structure
1 distinct chain · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription TERMINATION/ANTITERMINATION protein nusa | protein | 371 | 39% helix, 27% strand | P32727 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.31 | 0.75 | 13 | empty |
| 2 | 52 | 0.30 | 0.76 | 15 | empty |
Compared structures
- 2MT4 · Solution structure of the N-terminal domain of NUSA from B. Subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.31
- 2MT4 · Solution structure of the N-terminal domain of nusa from B. subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.31
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 P32727
- Elsewhere: UniProt P32727 · AlphaFold DB P32727
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