Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein PNEC_1620 (B1XS59)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein PNEC_1620… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1XS59
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7E60B954e5d9c3fdcf523d6f27d5Ced1637C0C0D
- Molecule
- Nucleotide-binding protein PNEC_1620
- UniProt
- B1XS59
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein PNEC_1620 | protein | 296 | 47% helix, 18% strand | B1XS59 |
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 | 182 | 0.52 | 0.78 | 28 | empty |
| 2 | 76 | 0.39 | 0.79 | 14 | empty |
| 3 | 65 | 0.37 | 0.79 | 13 | empty |
| 4 | 79 | 0.31 | 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 B1XS59
- Elsewhere: UniProt B1XS59 · AlphaFold DB B1XS59
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.