Research workbench
Phencyclidine-bound GLUN1A-GLUN2B NMDA receptors
Analyse Phencyclidine-bound GLUN1A-GLUN2B NMDA receptors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SAB
- Type
- protein
- Length
- 3,160 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor ionotropic, NMDA 1; Glutamate receptor ionotropic, NMDA 2B
- UniProt
- P35439, Q00960
- Ligands
- 1PC, NAG
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor ionotropic, NMDA 1 | protein | 795 | 37% helix, 17% strand | P35439 |
| B, D | Glutamate receptor ionotropic, NMDA 2B | protein | 785 | 37% helix, 15% strand | Q00960 |
Ligands and binding sites
- 1PC · 1-(phenyl-1-cyclohexyl)piperidine · ligand · chains A, B, C, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains B, D, A, C
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 | 956 | 0.86 | 0.86 | 94 | 1PC |
| 2 | 950 | 0.82 | 0.83 | 134 | empty |
| 3 | 434 | 0.82 | 0.89 | 78 | empty |
| 4 | 455 | 0.82 | 0.89 | 77 | empty |
| 5 | 1025 | 0.82 | 0.83 | 100 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2985 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 2964 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 2786 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 2696 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 80 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 disulfide, 5 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 P35439
- Every structure of UniProt Q00960
- Elsewhere: RCSB PDB 7SAB · PDBe 7SAB · UniProt P35439 · UniProt Q00960
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.