MolNFT v1 · #144428 · protein
Human MGLU8 receptor complexed with L-AP4
6BT5 · Metabotropic glutamate receptor 8: “Human MGLU8 receptor complexed with L-AP4”. X-ray diffraction, 2 ligands (E7P, NAG), 8 pockets (best druggability 0.78). MolNFT v1 #144428 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6BT5
- Type
- protein
- Length
- 875 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metabotropic glutamate receptor 8
- UniProt
- O00222
- Ligands
- E7P, NAG
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metabotropic glutamate receptor 8 | protein | 442 | 35% helix, 20% strand | O00222 |
| B | Metabotropic glutamate receptor 8 | protein | 433 | 35% helix, 22% strand | O00222 |
Ligands and binding sites
- E7P · (2S)-2-amino-4-phosphonobutanoic acid · 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.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 339 | 0.78 | 0.89 | 61 | E7P |
| 2 | 692 | 0.78 | 0.83 | 58 | empty |
| 3 | 325 | 0.76 | 0.88 | 55 | E7P |
| 4 | 193 | 0.60 | 0.82 | 30 | empty |
| 5 | 83 | 0.56 | 0.86 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 794 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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 O00222
- Elsewhere: RCSB PDB 6BT5 · PDBe 6BT5 · UniProt O00222
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