Research workbench
Structure of GLUA2-lbd in complex with mes
Analyse Structure of GLUA2-lbd in complex with mes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H8J
- Type
- protein
- Length
- 1,039 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- SO4
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor 2 | protein | 261 | 38% helix, 21% strand | P19491 |
| B | Glutamate receptor 2 | protein | 259 | 38% helix, 21% strand | P19491 |
| D | Glutamate receptor 2 | protein | 258 | 39% helix, 22% strand | P19491 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, D, B, C
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 880 | 0.82 | 0.84 | 116 | MES, SO4, EDO |
| 2 | 618 | 0.78 | 0.84 | 82 | SO4, EDO |
| 3 | 331 | 0.69 | 0.82 | 50 | MES, SO4 |
| 4 | 553 | 0.68 | 0.78 | 52 | EDO |
| 5 | 370 | 0.64 | 0.79 | 37 | empty |
Interfaces
4 interfaces between chains.
- A–B · 913 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 906 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 491 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 348 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4H8J · Structure of GluA2-LBD in complex with MES · 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 4H8J · PDBe 4H8J · UniProt P19491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.