MolNFT v1 · #79661 · protein
Cnqx bound to an oxidized double cysteine mutant (A452C/S652C) of the ligand binding domain of GLUA2
3T9U · Glutamate receptor 2: “Cnqx bound to an oxidized double cysteine mutant (A452C/S652C) of the ligand binding domain of GLUA2”. X-ray diffraction, 2 ligands (CNI, ZN), 9 pockets (best druggability 0.79). MolNFT v1 #79661 on GenesisL1…
- PDB
- 3T9U
- Type
- protein
- Length
- 774 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- CNI, ZN
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate receptor 2 | protein | 258 | 36% helix, 21% strand | P19491 |
Ligands and binding sites
- CNI · 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.79 | 0.81 | 125 | empty |
| 2 | 79 | 0.76 | 0.98 | 22 | CNI |
| 3 | 68 | 0.74 | 0.99 | 20 | CNI |
| 4 | 70 | 0.73 | 0.97 | 21 | CNI |
| 5 | 180 | 0.60 | 0.83 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1053 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 284 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 80 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3T9U · CNQX bound to an oxidized double cysteine mutant (A452C/S652C) of the ligand binding… · 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 3T9U · PDBe 3T9U · UniProt P19491
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