Research workbench
Diheteromeric NMDA receptor GLUN1/GLUN2A in the '2-knuckle-symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 millimolar edta, and at pH 7.4
Analyse Diheteromeric NMDA receptor GLUN1/GLUN2A in the '2-knuckle-symmetric'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MMG
- Type
- protein
- Length
- 3,054 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor ionotropic, NMDA 1; Glutamate receptor ionotropic, NMDA 2A
- UniProt
- P35439, Q00959
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 4 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor ionotropic, NMDA 1 | protein | 768 | 38% helix, 17% strand | P35439 |
| B | Glutamate receptor ionotropic, NMDA 2A | protein | 760 | 35% helix, 15% strand | Q00959 |
| C | Glutamate receptor ionotropic, NMDA 1 | protein | 765 | 39% helix, 18% strand | P35439 |
| D | Glutamate receptor ionotropic, NMDA 2A | protein | 761 | 36% helix, 16% strand | Q00959 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 42 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 | 1188 | 0.88 | 0.89 | 137 | empty |
| 2 | 985 | 0.85 | 0.86 | 116 | empty |
| 3 | 1158 | 0.84 | 0.85 | 121 | empty |
| 4 | 1154 | 0.80 | 0.82 | 115 | empty |
| 5 | 967 | 0.79 | 0.81 | 83 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3665 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 3516 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 2566 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 2416 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 456 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 34 glycan, 10 disulfide (N-glycosylation, disulfide).
Compared structures
- 6MMG · Diheteromeric NMDA receptor GluN1/GluN2A in the '2-Knuckle-Symmetric' conformation, in… · the same entry in another collection · chain D against D, TM-score 1.00
- P35439 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, NMDA 1 (P35439) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q00959 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, NMDA 2A (Q00959) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 Q00959
- Elsewhere: RCSB PDB 6MMG · PDBe 6MMG · UniProt P35439 · UniProt Q00959
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.