MolNFT v1 · #138300 · protein
Activated GLUA2 complex bound to glutamate, cyclothiazide, and stz in digitonin
5WEO: “Activated GLUA2 complex bound to glutamate, cyclothiazide, and stz in digitonin”. Electron microscopy, 1 ligand (CYZ). MolNFT v1 #138300 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5WEO
- Type
- protein
- Length
- 3,954 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19491, O88602
- Ligands
- CYZ
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 989 | — | P19491, O88602 |
| B, D | — | protein | 988 | — | P19491, O88602 |
Ligands and binding sites
- CYZ · Cyclothiazide · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WEO · Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin · the same entry in another collection · chain A against A, TM-score 1.00
- O88602 · AlphaFold monomer V2.0 prediction for voltage-dependent calcium channel gamma-2 subunit… · a predicted model of the same protein · chain D against A, TM-score 0.19
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
- Every structure of UniProt O88602
- Elsewhere: RCSB PDB 5WEO · PDBe 5WEO · UniProt P19491 · UniProt O88602
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