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: 4F11
Type: protein
Length: 417 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
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gamma-aminobutyric acid type B receptor subunit 2	protein	417	40% helix, 22% strand	O75899

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.71	0.98	27	empty
2	143	0.51	0.80	21	empty
3	120	0.46	0.78	17	empty
4	53	0.39	0.82	19	empty
5	78	0.32	0.74	20	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4F11 · 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 0.97

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 4F11 · PDBe 4F11 · UniProt O75899

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.