Research workbench
Crystal structure of the GLUK2EM lbd dimer assembly complex with 2S, 4R-4-methylglutamate
Analyse Crystal structure of the GLUK2EM lbd dimer assembly complex with 2S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CMM
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor ionotropic, kainate 2
- UniProt
- P42260, Q13002
- Ligands
- SYM
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor ionotropic, kainate 2 | protein | 257 | 39% helix, 21% strand | P42260, Q13002 |
Ligands and binding sites
- SYM · 2S,4R-4-methylglutamate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.73 | 0.98 | 19 | SYM |
| 2 | 102 | 0.40 | 0.76 | 21 | empty |
| 3 | 99 | 0.39 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5CMM · Crystal structure of the GluK2EM LBD dimer assembly complex with 2S,4R-4-methylglutamate · the same entry in another collection · chain A against A, TM-score 1.00
- P42260 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 2 (P42260) · a predicted model of the same protein · chain A against A, TM-score 0.94
- Q13002 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 2 (Q13002) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P42260
- Every structure of UniProt Q13002
- Elsewhere: RCSB PDB 5CMM · PDBe 5CMM · UniProt P42260 · UniProt Q13002
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