Research workbench
Structure of GLUA2* in complex with competitive antagonist zk 200775
Analyse Structure of GLUA2* in complex with competitive antagonist zk 200775 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U4G
- Type
- protein
- Length
- 3,072 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- ZK1, NAG, BMA
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutamate receptor 2 | protein | 768 | 38% helix, 17% strand | P19491 |
Ligands and binding sites
- ZK1 · {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid · ligand · 4 copies · chains A, B, C, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 8 copies · chains 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 | 1062 | 0.82 | 0.83 | 123 | ZK1 |
| 2 | 992 | 0.81 | 0.83 | 101 | ZK1 |
| 3 | 672 | 0.76 | 0.81 | 61 | empty |
| 4 | 695 | 0.75 | 0.80 | 78 | empty |
| 5 | 571 | 0.73 | 0.81 | 59 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3228 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 3098 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 2770 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 2608 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 467 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 4U4G · Structure of GluA2* in complex with competitive antagonist ZK 200775 · 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 4U4G · PDBe 4U4G · UniProt P19491
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