Research workbench
Full length GluA2-FW-(R,R)-2b complex
Analyse Full length GluA2-FW-(R,R)-2b complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U1Y
- Type
- protein
- Length
- 2,908 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.8999
- Source
- Rattus norvegicus
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- FWD, FWF, NAG
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · resolution 3.8999 · 4 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 720 | 43% helix, 19% strand | P19491 |
| B | Glutamate receptor 2 | protein | 731 | 42% helix, 18% strand | P19491 |
| C | Glutamate receptor 2 | protein | 730 | 42% helix, 18% strand | P19491 |
| D | Glutamate receptor 2 | protein | 727 | 42% helix, 17% strand | P19491 |
Ligands and binding sites
- FWD · 2-amino-3-(5-fluoro-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-propionic acid · ligand · 4 copies · chains A, B, C, D
- FWF · N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide · ligand · 2 copies · chains A, D, B, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.81 | 0.83 | 94 | FWF |
| 2 | 1025 | 0.79 | 0.81 | 98 | empty |
| 3 | 930 | 0.79 | 0.81 | 94 | FWF |
| 4 | 119 | 0.76 | 0.95 | 32 | empty |
| 5 | 687 | 0.75 | 0.80 | 62 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2925 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 2727 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 2195 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 2191 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 450 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 4U1Y · Full length GLUA2-fw-(R,R)-2B complex · 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 P19491
- Elsewhere: RCSB PDB 4U1Y · PDBe 4U1Y · UniProt P19491
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