Research workbench
AlphaFold monomer V2.0 prediction for neuropeptide Y receptor type 1 (Q1RMU8)
Analyse AlphaFold monomer V2.0 prediction for neuropeptide Y receptor type 1 (Q1RMU8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1RMU8
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1fA013812fF4972aC7cbC0aBe90577F81d14A577
- Molecule
- Neuropeptide Y receptor type 1
- UniProt
- Q1RMU8
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuropeptide Y receptor type 1 | protein | 383 | 72% helix, 2% strand | Q1RMU8 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.80 | 0.82 | 63 | empty |
| 2 | 277 | 0.60 | 0.79 | 35 | empty |
| 3 | 247 | 0.58 | 0.79 | 34 | empty |
| 4 | 63 | 0.36 | 0.77 | 12 | empty |
Modifications
Observed in the structure: 2 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 Q1RMU8
- Elsewhere: UniProt Q1RMU8 · AlphaFold DB Q1RMU8
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