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AlphaFold monomer V2.0 prediction for RAS/RAP GTPase-activating protein syngap (F6SEU4)
Analyse AlphaFold monomer V2.0 prediction for RAS/RAP GTPase-activating protein syngap… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F6SEU4
- Type
- protein
- Length
- 1,340 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- RAS/RAP GTPase-activating protein syngap
- UniProt
- F6SEU4
- Pockets
- 8 · best druggability 0.81
Structure
1 distinct chain · 30% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS/RAP GTPase-activating protein syngap | protein | 1340 | 30% helix, 8% strand | F6SEU4 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.81 | 0.84 | 106 | empty |
| 2 | 454 | 0.62 | 0.76 | 35 | empty |
| 3 | 146 | 0.56 | 0.82 | 24 | empty |
| 4 | 255 | 0.55 | 0.77 | 38 | empty |
| 5 | 86 | 0.54 | 0.85 | 19 | 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 F6SEU4
- Elsewhere: UniProt F6SEU4 · AlphaFold DB F6SEU4
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