Research workbench
AlphaFold monomer V2.0 prediction for nuclease sbccd subunit D (Q5HPJ4)
Analyse AlphaFold monomer V2.0 prediction for nuclease sbccd subunit D (Q5HPJ4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5HPJ4
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78a503a9F23864BFbc868D392a218431330dD1fd
- Molecule
- Nuclease sbccd subunit D
- UniProt
- Q5HPJ4
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclease sbccd subunit D | protein | 374 | 34% helix, 24% strand | Q5HPJ4 |
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 | 57 | 0.74 | 0.99 | 16 | empty |
| 2 | 163 | 0.52 | 0.78 | 20 | empty |
| 3 | 80 | 0.34 | 0.75 | 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 Q5HPJ4
- Elsewhere: UniProt Q5HPJ4 · AlphaFold DB Q5HPJ4
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