Research workbench
AlphaFold monomer V2.0 prediction for GTPase obg (Q12F99)
Analyse AlphaFold monomer V2.0 prediction for GTPase obg (Q12F99) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12F99
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x817FafA0D4e279Fbf0B85cd3Ceb78B2E511A008e
- Molecule
- GTPase obg
- UniProt
- Q12F99
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 25% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase obg | protein | 361 | 25% helix, 24% strand | Q12F99 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.66 | 0.94 | 18 | empty |
| 2 | 184 | 0.61 | 0.82 | 27 | empty |
| 3 | 185 | 0.50 | 0.77 | 19 | empty |
| 4 | 74 | 0.37 | 0.77 | 15 | empty |
| 5 | 53 | 0.30 | 0.76 | 11 | 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 Q12F99
- Elsewhere: UniProt Q12F99 · AlphaFold DB Q12F99
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