MolNFT v1 · #268418 · protein
AlphaFold monomer V2.0 prediction for neuropeptide Y receptor type 1 (P25929)
P25929: “AlphaFold monomer V2.0 prediction for neuropeptide Y receptor type 1 (P25929)”. 5 pockets (best druggability 0.80). MolNFT v1 #268418 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P25929
- Type
- protein
- Length
- 384 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Neuropeptide Y receptor type 1
- UniProt
- P25929
- Pockets
- 5 · best druggability 0.80
Structure
1 distinct chain · 71% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuropeptide Y receptor type 1 | protein | 384 | 71% helix, 3% strand | P25929 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.80 | 0.82 | 60 | empty |
| 2 | 198 | 0.56 | 0.79 | 29 | empty |
| 3 | 239 | 0.55 | 0.77 | 31 | empty |
| 4 | 73 | 0.43 | 0.81 | 12 | empty |
| 5 | 59 | 0.35 | 0.77 | 10 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5ZBH · The crystal structure of human neuropeptide Y Y1 receptor with bms- 193885 · an experimental structure of the same protein · chain A against A, TM-score 0.75
- 7X9A · Cryo-EM structure of neuropeptide Y Y1 receptor in complex with npy and gi · an experimental structure of the same protein · chain A against R, TM-score 0.73
- 8K6M · Structural complex of neuropeptide Y receptor 1 · an experimental structure of the same protein · chain A against D, TM-score 0.71
- 5ZBQ · The crystal structure of human neuropeptide Y Y1 receptor with ur- MK299 · an experimental structure of the same protein · chain A against A, TM-score 0.71
- 7VGX · Neuropeptide Y Y1 receptor (NPY1R) in complex with G protein and its endogeneous… · an experimental structure of the same protein · chain A against R, TM-score 0.68
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 P25929
- Elsewhere: UniProt P25929 · AlphaFold DB P25929
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