Research workbench

Luteinizing HORMONE/CHORIOGONADOTROPIN RECEPTOR(S277I)-chorionic gonadotropin-gs-ORG43553 complex

Analyse Luteinizing HORMONE/CHORIOGONADOTROPIN RECEPTOR(S277I)-chorionic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FIH
Type: protein
Length: 1,381 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Engineered guanine nucleotide-binding protein G(S) subunit alpha; Guanine…
UniProt: P54311, P63212, P22888, P01215, P0DN86
Ligands: 55Z
Pockets: 18 · best druggability 0.84

Structure

electron microscopy · 6 distinct chains · 29% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Engineered guanine nucleotide-binding protein G(S) subunit alpha	protein	238	45% helix, 14% strand	—
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	338	8% helix, 43% strand	P54311
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	57	54% helix, 0% strand	P63212
R	Lutropin-choriogonadotropic hormone receptor	protein	550	42% helix, 13% strand	P22888
X	Glycoprotein hormones alpha chain	protein	88	5% helix, 55% strand	P01215
Y	Choriogonadotropin subunit beta 3	protein	110	0% helix, 49% strand	P0DN86

Ligands and binding sites

55Z · 5-azanyl-N-tert-butyl-2-methylsulfanyl-4-[3-(2-morpholin-4-ylethanoylamino)phenyl]thieno[2,3-d]pyrimidine-6-carboxamide · ligand · chains R

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

Pockets

18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.84	0.91	50	55Z
2	652	0.81	0.85	56	empty
3	287	0.74	0.87	35	empty
4	55	0.70	0.98	25	empty
5	655	0.67	0.76	70	empty

Interfaces

7 interfaces between chains.

X–Y · 2220 Å² buried · 35 hydrogen bonds · protein-protein
B–G · 2220 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1508 Å² buried · 15 hydrogen bonds · protein-protein
A–R · 1215 Å² buried · 13 hydrogen bonds · protein-protein
R–X · 947 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

7FIH · luteinizing hormone/choriogonadotropin receptor(S277I)-chorionic gonadotropin-Gs-Org43553… · the same entry in another collection · chain Y against Y, 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 0.99
P22888 · AlphaFold monomer V2.0 prediction for lutropin-choriogonadotropic hormone receptor… · a predicted model of the same protein · chain R against A, TM-score 0.94
P01215 · AlphaFold monomer V2.0 prediction for glycoprotein hormones alpha chain (P01215) · a predicted model of the same protein · chain X against A, TM-score 0.94
P0DN86 · AlphaFold monomer V2.0 prediction for choriogonadotropin subunit beta 3 (P0DN86) · a predicted model of the same protein · chain Y against A, TM-score 0.90
P63212 · 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 0.66

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 P63212
Every structure of UniProt P22888
Every structure of UniProt P01215
Every structure of UniProt P0DN86
Elsewhere: RCSB PDB 7FIH · PDBe 7FIH · UniProt P54311 · UniProt P63212 · UniProt P22888 · UniProt P01215 · UniProt P0DN86

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