Research workbench
GLUA2-0XGSG1L bound to zk
Analyse GLUA2-0XGSG1L bound to zk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VHW
- Type
- protein
- Length
- 3,126 residues
- Chains
- 4
- 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
- ZK1, NAG
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 43% 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 | 44% helix, 17% strand | P19491, D3ZK93 |
| B, D | Glutamate receptor 2,GERM cell-specific gene 1-like protein | protein | 780 | 42% helix, 15% strand | P19491, D3ZK93 |
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 · 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 | 1015 | 0.86 | 0.86 | 115 | empty |
| 2 | 363 | 0.85 | 0.94 | 28 | empty |
| 3 | 1062 | 0.84 | 0.85 | 128 | empty |
| 4 | 106 | 0.78 | 0.98 | 32 | empty |
| 5 | 685 | 0.77 | 0.83 | 67 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3526 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 3512 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 3389 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 3314 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 412 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 5VHW · PDBe 5VHW · UniProt P19491 · UniProt D3ZK93
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