Research workbench
AlphaFold monomer V2.0 prediction for ran-specific GTPase-activating protein 30 (P53107)
Analyse AlphaFold monomer V2.0 prediction for ran-specific GTPase-activating protein 30… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P53107
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF3dC0C0AfbCaFe21EC13288d7b1F1aD875Dd78F1
- Molecule
- Ran-specific GTPase-activating protein 30
- UniProt
- P53107
- Pockets
- 6 · best druggability 0.75
Structure
1 distinct chain · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ran-specific GTPase-activating protein 30 | protein | 440 | 55% helix, 15% strand | P53107 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.75 | 0.95 | 18 | empty |
| 2 | 672 | 0.67 | 0.76 | 74 | empty |
| 3 | 159 | 0.46 | 0.76 | 24 | empty |
| 4 | 99 | 0.37 | 0.76 | 19 | empty |
| 5 | 113 | 0.35 | 0.73 | 18 | 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 P53107
- Elsewhere: UniProt P53107 · AlphaFold DB P53107
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