Research workbench
AlphaFold monomer V2.0 prediction for segregation and condensation protein a (Q03MF6)
Analyse AlphaFold monomer V2.0 prediction for segregation and condensation protein a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q03MF6
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Segregation and condensation protein a
- UniProt
- Q03MF6
- Pockets
- 1 · best druggability 0.30
Structure
1 distinct chain · 58% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Segregation and condensation protein a | protein | 237 | 58% helix, 5% strand | Q03MF6 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.30 | 0.76 | 14 | 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 Q03MF6
- Elsewhere: UniProt Q03MF6 · AlphaFold DB Q03MF6
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