MolNFT v1 · #178353 · protein
Thermostabilised full length human MGLUR5-5M bound with L-quisqualic acid
7FD8: “Thermostabilised full length human MGLUR5-5M bound with L-quisqualic acid”. Electron microscopy, 3 ligands (QUS, Y01, NAG). MolNFT v1 #178353 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7FD8
- Type
- protein
- Length
- 1,528 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41594
- Ligands
- QUS, Y01, NAG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 764 | — | P41594 |
Ligands and binding sites
- QUS · (S)-2-amino-3-(3,5-dioxo-[1,2,4]oxadiazolidin-2-yl)-propionic acid · ligand · 2 copies · chains A, B
- Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7FD8 · Thermostabilised full length human mGluR5-5M bound with L-quisqualic acid · 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 0.94
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
- Elsewhere: RCSB PDB 7FD8 · PDBe 7FD8 · UniProt P41594
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