8QEG: G11 protein heterotrimer

Crystal structure of the G11 protein heterotrimer bound to YM-254890 inhibitor. Determined by X-ray diffraction at 1.7 Å resolution. Released 19 Mar 2025.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,952
Mol. weight: 88.7 kDa
Ligands: HF2, THC, ACE, OTH
Released: 19 Mar 2025

Explore 8QEG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QEG contains 31 α-helices and 36 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	13-36	24
β-strand	39-45	7	1
α-helix	52-63	12
α-helix	69-73	5
α-helix	76-96	21
α-helix	105-114	10
α-helix	118-120	3
α-helix	126-136	11
α-helix	139-146	8
α-helix	148-150	3
α-helix	157-162	6
α-helix	164-168	5
α-helix	176-181	6
β-strand	190-196	7	1
β-strand	199-205	7	1
α-helix	213-215	3
α-helix	217-220	4
β-strand	225-231	7	1
α-helix	232-236	5
β-strand	238-239	2	2
α-helix	240-242	3
β-strand	245-246	2	2
α-helix	247-260	14
α-helix	262-264	3
β-strand	268-274	7	1
α-helix	276-282	7
α-helix	288-290	3
α-helix	302-313	12
β-strand	324-328	5	1
α-helix	334-352	19

Chain B: 4 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	10-25	16
α-helix	30-34	5
α-helix	38-39	2
β-strand	47-51	5	3
β-strand	58-63	6	4
β-strand	69-74	6	4
β-strand	78-83	6	4
β-strand	89-94	6	4
β-strand	100-105	6	5
β-strand	111-116	6	5
β-strand	120-125	6	5
β-strand	135-140	6	5
β-strand	146-153	8	6
β-strand	156-161	6	6
β-strand	166-170	5	6
β-strand	175-180	6	6
β-strand	187-192	6	7
β-strand	198-203	6	7
β-strand	207-212	6	7
β-strand	218-223	6	7
β-strand	229-234	6	8
β-strand	240-245	6	8
β-strand	250-254	5	8
β-strand	259-264	6	8
α-helix	272	1
β-strand	273-278	6	9
β-strand	284-289	6	9
β-strand	293-298	6	9
β-strand	304-309	6	9
β-strand	315-320	6	3
β-strand	327-331	5	3
β-strand	336-339	4	3

Chain G: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	12-24	13
α-helix	31-45	15
α-helix	46-48	3
α-helix	54-56	3
α-helix	57-59	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein subunit alpha-11	A	protein	352	Homo sapiens	P29992 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	344	Homo sapiens	P62873 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Homo sapiens	P59768 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8QEG_1 Guanine nucleotide-binding protein subunit alpha-11 (chains A)
GCTLSAEDKAAVERSKMIDRNLREDGEKARRELKLLLLGTGESGKSTFIKQMRIIHGAGY
SEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQ
YVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTT
GIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENR
MEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAARE
FILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV

Sequence of entity 2 (B), FASTA

>8QEG_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
PGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLA
KIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGG
LDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQ
TTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFP
NGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNV
WDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>8QEG_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFSAIL

Ligands and cofactors

ID	Name	Formula	Copies
HF2	(2R)-2-hydroxy-3-phenylpropanoic acid	C9 H10 O3	1
THC	N-methylcarbonylthreonine	C6 H11 N O4	1
ACE	Acetyl group	C2 H4 O	1
OTH	N,O-dimethyl-L-threonine	C6 H13 N O3	1
DAM	N-methyl-alpha-beta-dehydroalanine	C4 H7 N O2	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
ALA	Alanine	C3 H7 N O2	1
MAA	N-methyl-L-alanine	C4 H9 N O2	1
HL2	(2S,3R)-2-amino-3-hydroxy-4-methylpentanoic acid	C6 H13 N O3	2

Water and common crystallization additives (EDO) are not listed.

Primary citation

Cyclic peptide inhibitors function as molecular glues to stabilize Gq/11 heterotrimers. Muhle, J., Alenfelder, J., Rodrigues, M.J. et al. Proc Natl Acad Sci U S A (2025) 122:e2418398122-e2418398122. DOI 10.1073/pnas.2418398122 · PubMed

Other PDB entries of the same protein (UniProt P29992 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8QEH 1.43 Å, Crystal structure of the G11 protein heterotrimer bound to FR900359 inhibitor
9P87 2.8 Å, NTSR1-G11-NTS(8-13) Complex in the Canonical, AHD Partially Closed State (C-P-Closed-Apo)
9UCP 2.88 Å, cryo-EM structure of M1 muscarinic acetylcholine receptor-alpha5 helix of G11 protein…
7XXH 2.9 Å, Cryo-EM structure of the purinergic receptor P2Y1R in complex with 2MeSADP and G11
9P86 2.9 Å, NTSR1-G11-NTS(8-13) Complex in the Canonical, AHD Open State (C-Open-Apo)
9P88 2.9 Å, NTSR1-G11-NTS(8-13) Complex in the Non-Canonical, AHD Open State (NC-Open-Apo)
6OIJ 3.3 Å, Muscarinic acetylcholine receptor 1-G11 protein complex
9UAP 3.62 Å, cryo-EM structure of ligand-free active-state M1 muscarinic acetylcholine receptor with…
7TRY 3.7 Å, Cryo-EM structure of corticotropin releasing factor receptor 2 bound to Urocortin 1 and…
9P8A 3.7 Å, NTSR1-G11-NTS(8-13) GTP-Bound Complex in the Canonical, AHD Closed State 3DVA Separated…
9P89 3.9 Å, NTSR1-G11-NTS(8-13) GTP-Bound Complex in the Canonical, AHD Closed State 3DVA Separated…
7RKF 4.0 Å, Structure of CX3CL1-US28-G11iN18-scFv16 in TL-state

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