Research workbench
AlphaFold monomer V2.0 prediction for GTPase obg (A5EVP4)
Analyse AlphaFold monomer V2.0 prediction for GTPase obg (A5EVP4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5EVP4
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC35EFAFBd6C1C86993de1c3D20c02e3f198163fB
- Molecule
- GTPase obg
- UniProt
- A5EVP4
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 24% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase obg | protein | 353 | 24% helix, 25% strand | A5EVP4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.58 | 0.83 | 20 | empty |
| 2 | 84 | 0.55 | 0.86 | 21 | empty |
| 3 | 165 | 0.50 | 0.78 | 22 | empty |
| 4 | 83 | 0.36 | 0.76 | 14 | 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 A5EVP4
- Elsewhere: UniProt A5EVP4 · AlphaFold DB A5EVP4
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