Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein PST_1028 (A4VIC4)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein PST_1028… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4VIC4
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9C80B506aC88CC4745F2CFbA143f406EBbF0Cf05
- Molecule
- Nucleotide-binding protein PST_1028
- UniProt
- A4VIC4
- Pockets
- 4 · best druggability 0.56
Structure
1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein PST_1028 | protein | 285 | 45% helix, 19% strand | A4VIC4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.56 | 0.82 | 24 | empty |
| 2 | 180 | 0.46 | 0.75 | 26 | empty |
| 3 | 51 | 0.26 | 0.74 | 12 | empty |
| 4 | 58 | 0.25 | 0.72 | 16 | 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 A4VIC4
- Elsewhere: UniProt A4VIC4 · AlphaFold DB A4VIC4
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