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AlphaFold monomer V2.0 prediction for small ribosomal subunit biogenesis GTPase rsga (B2THS4)
Analyse AlphaFold monomer V2.0 prediction for small ribosomal subunit biogenesis GTPase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2THS4
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2212E7C2D74dEcE3Be1026CF82bc07Dd6C6F59a9
- Molecule
- Small ribosomal subunit biogenesis GTPase rsga
- UniProt
- B2THS4
- Pockets
- 3 · best druggability 0.43
Structure
1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small ribosomal subunit biogenesis GTPase rsga | protein | 290 | 31% helix, 26% strand | B2THS4 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.43 | 0.80 | 15 | empty |
| 2 | 50 | 0.35 | 0.79 | 11 | empty |
| 3 | 75 | 0.30 | 0.73 | 20 | 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 B2THS4
- Elsewhere: UniProt B2THS4 · AlphaFold DB B2THS4
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