MolNFT v1 · #436521 · protein
AlphaFold monomer V2.0 prediction for serpentine receptor class gamma-20 (P91535)
P91535: “AlphaFold monomer V2.0 prediction for serpentine receptor class gamma-20 (P91535)”. 4 pockets (best druggability 0.80). MolNFT v1 #436521 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P91535
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Serpentine receptor class gamma-20
- UniProt
- P91535
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 74% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serpentine receptor class gamma-20 | protein | 346 | 74% helix, 4% strand | P91535 |
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 | 1084 | 0.80 | 0.81 | 88 | empty |
| 2 | 174 | 0.56 | 0.80 | 23 | empty |
| 3 | 64 | 0.46 | 0.83 | 16 | empty |
| 4 | 156 | 0.41 | 0.73 | 25 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P91535
- Elsewhere: UniProt P91535 · AlphaFold DB P91535
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