MolNFT v1 · #508515 · protein
AlphaFold monomer V2.0 prediction for uncharacterized peptidase SAUSA300_1654 (Q2FG30)
Q2FG30: “AlphaFold monomer V2.0 prediction for uncharacterized peptidase SAUSA300_1654 (Q2FG30)”. 3 pockets (best druggability 0.42). MolNFT v1 #508515 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q2FG30
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Uncharacterized peptidase SAUSA300_1654
- UniProt
- Q2FG30
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized peptidase SAUSA300_1654 | protein | 351 | 38% helix, 24% strand | Q2FG30 |
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 | 86 | 0.42 | 0.79 | 14 | empty |
| 2 | 121 | 0.42 | 0.76 | 18 | empty |
| 3 | 51 | 0.34 | 0.79 | 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 Q2FG30
- Elsewhere: UniProt Q2FG30 · AlphaFold DB Q2FG30
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