MolNFT v2 · #209126 · protein
cryo-EM structure of homomeric kainate receptor GluK2 in resting (apo) state
8F0O: “cryo-EM structure of homomeric kainate receptor GluK2 in resting (apo) state”. Electron microscopy at 2.99, 3 ligands (NAG, MAN, BMA). MolNFT v2 #209126 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8F0O
- Type
- protein
- Length
- 2,968 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.99
- Source
- Rattus norvegicus
- UniProt
- P42260
- Ligands
- NAG, MAN, BMA
Structure
electron microscopy · resolution 2.99 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 742 | — | P42260 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 20 copies · chains A, B, C, D
- MAN · alpha-D-mannopyranose · sugar · 12 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 6 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P42260 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 2 (P42260) · a predicted model of the same protein · chain C against A, TM-score 0.84
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
- Elsewhere: RCSB PDB 8F0O · PDBe 8F0O · UniProt P42260
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