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Full length GLUA2-kainate-(R,R)-2B complex crystal form B
Analyse Full length GLUA2-kainate-(R,R)-2B complex crystal form B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U1X
- Type
- protein
- Length
- 2,980 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- KAI, FWF, NAG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 743 | 41% helix, 19% strand | P19491 |
| B | Glutamate receptor 2 | protein | 738 | 41% helix, 17% strand | P19491 |
| C | Glutamate receptor 2 | protein | 755 | 42% helix, 18% strand | P19491 |
| D | Glutamate receptor 2 | protein | 744 | 42% helix, 18% strand | P19491 |
Ligands and binding sites
- KAI · 3-(carboxymethyl)-4-isopropenylproline · ligand · 4 copies · chains A, B, C, D
- FWF · N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide · ligand · 2 copies · chains B, C, A, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B, 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 | 1074 | 0.84 | 0.85 | 132 | KAI, FWF |
| 2 | 1137 | 0.80 | 0.81 | 115 | KAI, FWF |
| 3 | 915 | 0.78 | 0.81 | 74 | empty |
| 4 | 1152 | 0.78 | 0.80 | 96 | empty |
| 5 | 920 | 0.77 | 0.80 | 85 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3595 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 3268 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 2314 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 2073 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 1096 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 4 glycan (disulfide, N-glycosylation).
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
- Elsewhere: RCSB PDB 4U1X · PDBe 4U1X · UniProt P19491
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