MolNFT v1 · #177210 · protein

Cryo-EM structure of human GABA(B) receptor-gi protein complex

7EB2 · Guanine nucleotide-binding protein G(I) subunit alpha-1: “Cryo-EM structure of human GABA(B) receptor-gi protein complex”. Electron microscopy, 2 ligands (2C0, FN0), 20 pockets (best druggability 0.86). MolNFT v1 #177210 on…

PDB: 7EB2
Type: protein
Length: 2,337 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanine nucleotide-binding protein G(I) subunit alpha-1; Guanine nucleotide-binding…
UniProt: P63096, P62873, P59768, Q9UBS5, O75899
Ligands: 2C0, FN0
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 6 distinct chains · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanine nucleotide-binding protein G(I) subunit alpha-1	protein	352	51% helix, 12% strand	P63096
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	339	7% helix, 46% strand	P62873
Y	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	57	58% helix, 0% strand	P59768
N	SCFV16	protein	231	5% helix, 46% strand	—
C	Gamma-aminobutyric acid type B receptor subunit 1	protein	678	49% helix, 15% strand	Q9UBS5
D	Gamma-aminobutyric acid type B receptor subunit 2	protein	680	50% helix, 15% strand	O75899

Ligands and binding sites

2C0 · baclofen · ligand · chains C
FN0 · (3S)-5,7-ditert-butyl-3-oxidanyl-3-(trifluoromethyl)-1-benzofuran-2-one · ligand · chains 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, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	786	0.86	0.88	62	empty
2	754	0.85	0.87	81	empty
3	1143	0.84	0.84	92	empty
4	925	0.80	0.82	97	empty
5	526	0.74	0.82	52	empty

Interfaces

7 interfaces between chains.

B–Y · 2148 Å² buried · 17 hydrogen bonds · protein-protein
C–D · 1966 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1191 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 802 Å² buried · 9 hydrogen bonds · protein-protein
A–N · 576 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

7EB2 · Cryo-EM structure of human GABA(B) receptor-Gi protein complex · the same entry in another collection · chain D against D, TM-score 1.00
P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain B against A, TM-score 0.99
P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain Y against A, TM-score 0.95
O75899 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid type B receptor subunit 2… · a predicted model of the same protein · chain D against A, TM-score 0.84
Q9UBS5 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid type B receptor subunit 1… · a predicted model of the same protein · chain C against A, TM-score 0.76
P63096 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.58

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 P63096
Every structure of UniProt P62873
Every structure of UniProt P59768
Every structure of UniProt Q9UBS5
Every structure of UniProt O75899
Elsewhere: RCSB PDB 7EB2 · PDBe 7EB2 · UniProt P63096 · UniProt P62873 · UniProt P59768 · UniProt Q9UBS5 · UniProt O75899

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