Research workbench
Native AMPA receptor
Analyse Native AMPA receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LDD
- Type
- protein
- Length
- 4,990 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P23818, G5E8H1, O35089, Q8VHW2
- Ligands
- D10, D12, C14, ZK1, HP6, R16, XVD, NAG
Structure
electron microscopy · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 776 | — | P23818 |
| B, D | — | protein | 778 | — | G5E8H1 |
| E, F | — | protein | 124 | — | O35089 |
| G, H | — | protein | 162 | — | Q8VHW2 |
| I, L | — | protein | 229 | — | — |
| J, M | — | protein | 211 | — | — |
| K, N | — | protein | 215 | — | — |
Ligands and binding sites
- D10 · Decane · ligand · 6 copies · chains A, C, F
- D12 · Dodecane · ligand · 6 copies · chains B, C, A, D, G, H
- C14 · Tetradecane · ligand · 6 copies · chains A, B, C, D, G, H
- 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
- HP6 · Heptane · ligand · 4 copies · chains A, G, C, H
- R16 · Hexadecane · ligand · 2 copies · chains A, C
- XVD · 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol · ligand · 2 copies · chains A, G, C, H
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains A, B, C, D
- OCT · N-octane · additive · 6 copies · chains B, D, A, G, C, H
- DD9 · nonane · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LDD · native AMPA receptor · the same entry in another collection · chain N against N, 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 P23818
- Every structure of UniProt G5E8H1
- Every structure of UniProt O35089
- Every structure of UniProt Q8VHW2
- Elsewhere: RCSB PDB 7LDD · PDBe 7LDD · UniProt P23818 · UniProt G5E8H1 · UniProt O35089 · UniProt Q8VHW2
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