Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein RPIC_0258 (B2UES4)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein RPIC_0258… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2UES4
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdacb7C9769309e46da3ccf02C1e79fC50894f529
- Molecule
- Nucleotide-binding protein RPIC_0258
- UniProt
- B2UES4
- Pockets
- 5 · best druggability 0.48
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein RPIC_0258 | protein | 297 | 47% helix, 18% strand | B2UES4 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.48 | 0.76 | 25 | empty |
| 2 | 130 | 0.46 | 0.78 | 18 | empty |
| 3 | 81 | 0.38 | 0.78 | 20 | empty |
| 4 | 63 | 0.29 | 0.73 | 14 | empty |
| 5 | 58 | 0.28 | 0.74 | 17 | 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 B2UES4
- Elsewhere: UniProt B2UES4 · AlphaFold DB B2UES4
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