Research workbench
Crystal Structure of the AvGluR1 ligand binding domain complex with glutamate at 1.37 Angstrom resolution
Analyse Crystal Structure of the AvGluR1 ligand binding domain complex with glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IO2
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.37
- Source
- Adineta vaga
- Molecule
- Glutamate receptor 1
- UniProt
- E9P5T5
- Ligands
- GLU, CL
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.37 · 2 distinct chains · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 1 | protein | 242 | 36% helix, 26% strand | E9P5T5 |
| B | Glutamate receptor 1 | protein | 242 | 36% helix, 26% strand | E9P5T5 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 4 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 | 249 | 0.75 | 0.89 | 44 | CL |
| 2 | 487 | 0.71 | 0.81 | 76 | empty |
| 3 | 155 | 0.55 | 0.81 | 29 | empty |
| 4 | 178 | 0.54 | 0.79 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4IO2 · Crystal structure of the AVGLUR1 ligand binding domain complex with glutamate at 1.37… · the same entry in another collection · chain A against A, TM-score 1.00
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 E9P5T5
- Elsewhere: RCSB PDB 4IO2 · PDBe 4IO2 · UniProt E9P5T5
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