Research workbench
Crystal structure of the extracellular domain of human GABA(B) receptor GBR2
Analyse Crystal structure of the extracellular domain of human GABA(B) receptor GBR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F12
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-aminobutyric acid type B receptor subunit 2
- UniProt
- O75899
- Ligands
- NAG, FUC
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-aminobutyric acid type B receptor subunit 2 | protein | 410 | 39% helix, 22% strand | O75899 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.64 | 0.78 | 60 | empty |
| 2 | 145 | 0.44 | 0.76 | 19 | empty |
| 3 | 62 | 0.37 | 0.79 | 20 | empty |
Modifications
Observed in the structure: 4 glycan, 3 disulfide (N-glycosylation, disulfide).
Compared structures
- 4F12 · Crystal structure of the extracellular domain of human GABA(B) receptor GBR2 · the same entry in another collection · chain A against A, TM-score 1.00
- O75899 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid type B receptor subunit 2… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O75899
- Elsewhere: RCSB PDB 4F12 · PDBe 4F12 · UniProt O75899
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