7E5E: GDP-bound GNAS

Crystal structure of GDP-bound GNAS in complex with the cyclic peptide inhibitor GD20. Determined by X-ray diffraction at 1.95 Å resolution. Released 2 Mar 2022.

Method: X-ray diffraction
Resolution: 1.95 Å
Organisms: Homo sapiens, synthetic construct
Chains: 8
Atoms: 11,740
Mol. weight: 171.38 kDa
Ligands: GDP
Released: 2 Mar 2022

Explore 7E5E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7E5E contains 84 α-helices and 40 β-strands across 8 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: 21 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	40-46	7	1
α-helix	53-64	12
α-helix	92-112	21
α-helix	122-124	3
α-helix	125-133	9
α-helix	144-154	11
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	194-199	6
β-strand	206-214	9	1
β-strand	217-226	10	1
β-strand	229	1	2
α-helix	231-238	8
β-strand	241-249	9	1
α-helix	250-252	3
β-strand	256	1	3
β-strand	264	1	3
α-helix	265-277	13
α-helix	280-282	3
β-strand	286-292	7	1
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-317	5
α-helix	326-327	2
α-helix	332-351	20
β-strand	359-363	5	1
α-helix	369-384	16
α-helix	386-391	6

Chain B: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	40-46	7	4
α-helix	53-64	12
α-helix	92-112	21
α-helix	122-124	3
α-helix	125-133	9
α-helix	144-154	11
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	194-199	6
β-strand	206-213	8	4
β-strand	218-226	9	4
β-strand	229	1	5
α-helix	234-238	5
β-strand	243-249	7	4
α-helix	250-254	5
β-strand	256	1	6
β-strand	264	1	6
α-helix	265-277	13
α-helix	280-282	3
β-strand	286-292	7	4
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-317	5
α-helix	326-327	2
α-helix	332-351	20
β-strand	359-363	5	4
α-helix	369-386	18

Chain C: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	39-46	8	7
α-helix	53-64	12
α-helix	92-112	21
α-helix	122-124	3
α-helix	125-133	9
α-helix	144-154	11
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	194-199	6
β-strand	206-214	9	7
β-strand	217-226	10	7
β-strand	229	1	8
α-helix	231-238	8
β-strand	241-249	9	7
α-helix	250-252	3
β-strand	256	1	9
β-strand	264	1	9
α-helix	265-277	13
α-helix	280-282	3
β-strand	286-292	7	7
α-helix	294-303	10
α-helix	308-310	3
α-helix	313-316	4
α-helix	332-349	18
β-strand	359-363	5	7
α-helix	369-389	21

Chain D: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	40-46	7	10
α-helix	53-64	12
α-helix	91-112	22
α-helix	122-124	3
α-helix	125-133	9
α-helix	144-154	11
α-helix	157-164	8
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-186	5
α-helix	194-199	6
β-strand	206-213	8	10
β-strand	218-226	9	10
β-strand	229	1	11
α-helix	231-238	8
β-strand	243-249	7	10
α-helix	250-254	5
β-strand	256	1	12
β-strand	264	1	12
α-helix	265-277	13
α-helix	280-282	3
β-strand	286-292	7	10
α-helix	294-301	8
α-helix	308-310	3
α-helix	313-317	5
α-helix	332-346	15
β-strand	359-363	5	10
α-helix	369-383	15

Chains E, F and H: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	3	1	2
α-helix	5-9	5

Chain G: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	3	1	8
α-helix	5-9	5
α-helix	12-14	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform Gnas-2 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	A, B, C, D	protein	348	Homo sapiens	P63092 (AlphaFold model)
GD20	E, F, G, H	protein	17	synthetic construct

Sequence of entity 1 (A, B, C, D), FASTA

>7E5E_1 Isoform Gnas-2 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains A, B, C, D)
GPQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGDSEKATKVQDIKNNLKEAIETI
VAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERS
NEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGG
QRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTIS
VILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFL
RISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL

Sequence of entity 2 (E, F, G, H), FASTA

>7E5E_2 GD20 (chains E, F, G, H)
XYLITFRQWAFNLPCGX

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	4

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

Primary citation

State-selective modulation of heterotrimeric G alpha s signaling with macrocyclic peptides. Dai, S.A., Hu, Q., Gao, R. et al. Cell (2022) 185:3950. DOI 10.1016/j.cell.2022.09.019 · PubMed

Other PDB entries of the same protein (UniProt P63092 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BPH 1.57 Å, Crystal structure of GppNHp-bound GNAS in complex with the cyclic peptide inhibitor GN13
6AU6 1.7 Å, Crystal structure of GDP-bound human GNAS R201C mutant
8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
7MBX 1.95 Å, Human Cholecystokinin 1 receptor (CCK1R) Gs complex
8F0J 2.0 Å, Calcitonin Receptor in complex with Gs and Pramlintide analogue peptide San45
8F2B 2.0 Å, Amylin 3 Receptor in complex with Gs and Pramlintide analogue peptide San45
9XXT 2.0 Å, Cryo-EM structure of lysophosphatidylserine (18:0)-bound GPR174-Gs complex
6X18 2.1 Å, GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor
6X19 2.1 Å, Non peptide agonist CHU-128, bound to Glucagon-Like peptide-1 (GLP-1) Receptor
9NTU 2.1 Å, Cryo-EM structure of BETP-GLP-1(9-36)-GLP-1R-Gs complex
7RTB 2.14 Å, Peptide-19 bound to the Glucagon-Like Peptide-1 Receptor (GLP-1R)
7TYF 2.2 Å, Human Amylin1 Receptor in complex with Gs and rat amylin peptide

Browse structure collections

About this viewer

MolViewer shows 7E5E directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.