MolNFT v2 · #223493 · protein
Human GluN1-2B with Fab 007-168
8VUU · Glutamate receptor ionotropic, NMDA 1: “Human GluN1-2B with Fab 007-168”. Electron microscopy at 4.05, 20 pockets (best druggability 0.84). MolNFT v2 #223493 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8VUU
- Type
- protein
- Length
- 4,026 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.05
- Source
- Homo sapiens
- Molecule
- Glutamate receptor ionotropic, NMDA 1; Glutamate receptor ionotropic, NMDA 2B; 007-168…
- UniProt
- Q05586, Q13224
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · resolution 4.05 · 6 distinct chains · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor ionotropic, NMDA 1 | protein | 802 | 36% helix, 10% strand | Q05586 |
| B | Glutamate receptor ionotropic, NMDA 2B | protein | 787 | 35% helix, 13% strand | Q13224 |
| D | Glutamate receptor ionotropic, NMDA 2B | protein | 784 | 36% helix, 12% strand | Q13224 |
| H | 007-168 Heavy | protein | 211 | 4% helix, 46% strand | — |
| J | 007-168 Heavy | protein | 210 | 3% helix, 45% strand | — |
| K, L | 007-168 Light | protein | 215 | 2% helix, 33% strand | — |
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 | 737 | 0.84 | 0.87 | 74 | empty |
| 2 | 1200 | 0.81 | 0.82 | 133 | empty |
| 3 | 513 | 0.78 | 0.85 | 98 | empty |
| 4 | 1189 | 0.77 | 0.79 | 102 | empty |
| 5 | 962 | 0.77 | 0.79 | 92 | empty |
Interfaces
14 interfaces between chains.
- A–B · 3109 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 2838 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 2648 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 2572 Ų buried · 1 hydrogen bond · protein-protein
- J–K · 1665 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide (disulfide).
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 Q05586
- Every structure of UniProt Q13224
- Elsewhere: RCSB PDB 8VUU · PDBe 8VUU · UniProt Q05586 · UniProt Q13224
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.