Research workbench

Human cholecystokinin 1 receptor (CCK1R) gq chimera (mgsqi) complex

Analyse Human cholecystokinin 1 receptor (CCK1R) gq chimera (mgsqi) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MBY
Type: protein
Length: 891 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1; Guanine…
UniProt: P54311, P59768, P06307, P32238, P63096, P63092
Ligands: Y01, NH2
Pockets: 8 · best druggability 0.82

Structure

electron microscopy · 5 distinct chains · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	339	8% helix, 45% strand	P54311
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	57	54% helix, 0% strand	P59768
P	Cholecystokinin-8	protein	8	0% helix, 0% strand	P06307
R	Cholecystokinin receptor type a	protein	283	78% helix, 5% strand	P32238
A	Guanine nucleotide-binding protein G(I) subunit alpha-1, guanine nucleotide-binding protein G(S) subunit alpha isoforms short, with certain residues mutated to match guanine nucleotide-binding protein G(Q) subunit	protein	204	47% helix, 18% strand	P63096, P63092

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · chains R
NH2 · Amino group · ion · chains P, R

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	572	0.82	0.87	57	empty
2	997	0.71	0.75	67	empty
3	87	0.52	0.84	16	empty
4	119	0.40	0.75	23	empty
5	85	0.37	0.76	24	empty

Interfaces

5 interfaces between chains.

B–G · 2219 Å² buried · 14 hydrogen bonds · protein-protein
R–A · 1064 Å² buried · 7 hydrogen bonds · protein-protein
B–A · 982 Å² buried · 11 hydrogen bonds · protein-protein
P–R · 981 Å² buried · 8 hydrogen bonds · protein-protein
B–R · 66 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, sulfation).

Compared structures

7MBY · Human Cholecystokinin 1 receptor (CCK1R) Gq chimera (mGsqi) complex · the same entry in another collection · chain A against A, TM-score 1.00
P54311 · 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 0.97
P32238 · AlphaFold monomer V2.0 prediction for cholecystokinin receptor type a (P32238) · a predicted model of the same protein · chain R against A, TM-score 0.94
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 G against A, TM-score 0.91
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 0.78
P06307 · AlphaFold monomer V2.0 prediction for cholecystokinin (P06307) · a predicted model of the same protein · chain P against A, TM-score 0.39

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 P54311
Every structure of UniProt P59768
Every structure of UniProt P06307
Every structure of UniProt P32238
Every structure of UniProt P63096
Every structure of UniProt P63092
Elsewhere: RCSB PDB 7MBY · PDBe 7MBY · UniProt P54311 · UniProt P59768 · UniProt P06307 · UniProt P32238 · UniProt P63096 · UniProt P63092

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