MolNFT v1 · #137224 · protein
GLUA2-2XGSG1L bound to L-quisqualate
5VHZ · Glutamate receptor 2,GERM cell-specific gene 1-like protein: “GLUA2-2XGSG1L bound to L-quisqualate”. Electron microscopy, 1 ligand (QUS), 20 pockets (best druggability 0.85). MolNFT v1 #137224 on GenesisL1: 3D structure, binding…
- PDB
- 5VHZ
- Type
- protein
- Length
- 3,484 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2,GERM cell-specific gene 1-like protein
- UniProt
- P19491, D3ZK93
- Ligands
- QUS
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 3 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor 2,GERM cell-specific gene 1-like protein | protein | 783 | 43% helix, 17% strand | P19491, D3ZK93 |
| B, D | Glutamate receptor 2,GERM cell-specific gene 1-like protein | protein | 780 | 42% helix, 16% strand | P19491, D3ZK93 |
| E, F | Glutamate receptor 2,GERM cell-specific gene 1-like protein | protein | 179 | 65% helix, 6% strand | P19491, D3ZK93 |
Ligands and binding sites
- QUS · (S)-2-amino-3-(3,5-dioxo-[1,2,4]oxadiazolidin-2-yl)-propionic acid · ligand · 4 copies · chains A, B, C, 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 | 354 | 0.85 | 0.94 | 28 | empty |
| 2 | 895 | 0.82 | 0.84 | 63 | empty |
| 3 | 1132 | 0.81 | 0.82 | 78 | empty |
| 4 | 670 | 0.78 | 0.83 | 67 | empty |
| 5 | 206 | 0.78 | 0.92 | 34 | empty |
Interfaces
10 interfaces between chains.
- C–D · 3399 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 3367 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 2492 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 2437 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 686 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 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 D3ZK93
- Elsewhere: RCSB PDB 5VHZ · PDBe 5VHZ · UniProt P19491 · UniProt D3ZK93
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