MolNFT v1 · #138298 · protein
GLUA2 bound to GSG1L in digitonin, state 1
5WEM · Chimera of glutamate receptor 2,GERM cell-specific gene 1…: “GLUA2 bound to GSG1L in digitonin, state 1”. Electron microscopy, 20 pockets (best druggability 0.88). MolNFT v1 #138298 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5WEM
- Type
- protein
- Length
- 3,484 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera of glutamate receptor 2,GERM cell-specific gene 1- like protein
- UniProt
- P19491, D3Z7H4
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 2 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Chimera of glutamate receptor 2,GERM cell-specific gene 1- like protein | protein | 962 | 46% helix, 15% strand | P19491, D3Z7H4 |
| B, D | Chimera of glutamate receptor 2,GERM cell-specific gene 1- like protein | protein | 780 | 40% helix, 17% strand | P19491, D3Z7H4 |
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 | 761 | 0.88 | 0.90 | 85 | empty |
| 2 | 678 | 0.85 | 0.89 | 95 | empty |
| 3 | 577 | 0.83 | 0.89 | 80 | empty |
| 4 | 715 | 0.80 | 0.85 | 93 | empty |
| 5 | 508 | 0.79 | 0.86 | 74 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3901 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 3890 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 3190 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 2842 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 410 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
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 D3Z7H4
- Elsewhere: RCSB PDB 5WEM · PDBe 5WEM · UniProt P19491 · UniProt D3Z7H4
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