Research workbench
Thermostabilised 7TM domain of human MGLU5 receptor bound to photoswitchable ligand alloswitch-1
Analyse Thermostabilised 7TM domain of human MGLU5 receptor bound to photoswitchable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P2L
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metabotropic glutamate receptor 5,ENDOLYSIN,METABOTROPIC glutamate receptor 5
- EC
- 3.2.1.17
- UniProt
- P41594, P00720
- Ligands
- 4YI
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metabotropic glutamate receptor 5,ENDOLYSIN,METABOTROPIC glutamate receptor 5 (EC 3.2.1.17) | protein | 414 | 71% helix, 4% strand | P41594, P00720 |
Ligands and binding sites
- 4YI · 2-chloranyl-~{N}-[2-methoxy-4-[(~{E})-pyridin-2-yldiazenyl]phenyl]benzamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.80 | 0.90 | 46 | 4YI |
| 2 | 453 | 0.66 | 0.78 | 47 | empty |
Modifications
Observed in the structure: 2 modified, 1 disulfide (alkylation, disulfide).
Compared structures
- 7P2L · thermostabilised 7TM domain of human mGlu5 receptor bound to photoswitchable ligand… · the same entry in another collection · chain A against A, TM-score 1.00
- P41594 · AlphaFold monomer V2.0 prediction for metabotropic glutamate receptor 5 (P41594) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 P41594
- Every structure of UniProt P00720
- Elsewhere: RCSB PDB 7P2L · PDBe 7P2L · UniProt P41594 · UniProt P00720
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