Research workbench
Crystal structure of metabotropic glutamate receptor subtype 1 complexed with an antagonist
Analyse Crystal structure of metabotropic glutamate receptor subtype 1 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ISS
- Type
- protein
- Length
- 904 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metabotropic glutamate receptor subtype 1
- UniProt
- P23385
- Ligands
- MCG
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Metabotropic glutamate receptor subtype 1 | protein | 452 | 36% helix, 19% strand | P23385 |
Ligands and binding sites
- MCG · (S)-(alpha)-methyl-4-carboxyphenylglycine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.62 | 0.77 | 48 | empty |
| 2 | 497 | 0.62 | 0.76 | 45 | MCG |
| 3 | 476 | 0.61 | 0.75 | 41 | MCG |
| 4 | 288 | 0.57 | 0.77 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 600 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1ISS · Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an… · the same entry in another collection · chain A against A, TM-score 1.00
- P23385 · AlphaFold monomer V2.0 prediction for metabotropic glutamate receptor 1 (P23385) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P23385
- Elsewhere: RCSB PDB 1ISS · PDBe 1ISS · UniProt P23385
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