MolNFT v1 · #124321 · protein
Cryo-EM structure of GLUA2-0XSTZ at 8.7 ångström resolution
5KBS · Glutamate receptor 2,VOLTAGE-dependent calcium channel…: “Cryo-EM structure of GLUA2-0XSTZ at 8.7 ångström resolution”. Electron microscopy, 2 ligands (ZK1, NAG), 20 pockets (best druggability 0.84). MolNFT v1 #124321 on GenesisL1…
- PDB
- 5KBS
- Type
- protein
- Length
- 3,119 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit
- UniProt
- P19491, O88602
- Ligands
- ZK1, NAG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit | protein | 782 | 40% helix, 17% strand | P19491, O88602 |
| B, C, D | Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit | protein | 779 | 40% helix, 17% strand | P19491, O88602 |
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 | 986 | 0.84 | 0.85 | 116 | ZK1 |
| 2 | 946 | 0.84 | 0.85 | 120 | ZK1 |
| 3 | 1127 | 0.79 | 0.80 | 121 | empty |
| 4 | 702 | 0.70 | 0.78 | 62 | empty |
| 5 | 503 | 0.70 | 0.80 | 55 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3011 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 2983 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 2601 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 2544 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 261 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 5KBS · Cryo-EM structure of GluA2-0xSTZ at 8.7 Angstrom resolution · the same entry in another collection · chain D against D, TM-score 1.00
- O88602 · AlphaFold monomer V2.0 prediction for voltage-dependent calcium channel gamma-2 subunit… · a predicted model of the same protein · chain A against A, TM-score 0.15
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 O88602
- Elsewhere: RCSB PDB 5KBS · PDBe 5KBS · UniProt P19491 · UniProt O88602
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