6AU6: GDP-bound human GNAS R201C mutant

Crystal structure of GDP-bound human GNAS R201C mutant. Determined by X-ray diffraction at 1.7 Å resolution. Released 9 May 2018.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,098
Mol. weight: 44.71 kDa
Ligands: GDP, MG
Released: 9 May 2018

Explore 6AU6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6AU6 contains 21 α-helices and 8 β-strands across 1 chain. 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	39-46	8	1
α-helix	53-64	12
α-helix	85-110	26
α-helix	122-124	3
α-helix	125-133	9
α-helix	144-154	11
α-helix	157-163	7
α-helix	166-168	3
α-helix	175-179	5
α-helix	182-185	4
α-helix	194-199	6
β-strand	207-214	8	1
β-strand	217-224	8	1
α-helix	228-237	10
β-strand	243-249	7	1
α-helix	250-252	3
β-strand	256	1	2
β-strand	264	1	2
α-helix	265-277	13
α-helix	280-282	3
β-strand	287-292	6	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	369-389	21
α-helix	390-392	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	A	protein	377	Homo sapiens	P63092 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6AU6_1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains A)
AHMSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRIL
HVNGFNGDSEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNV
PDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDL
LRCCVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQSFNDVTAIIFVVASSSYNMVI
REDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFAR
YTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFN
DCRDIIQRMHLRQYELL

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1

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

Primary citation

Disease-Causing Mutations in the G Protein G alpha s Subvert the Roles of GDP and GTP. Hu, Q., Shokat, K.M. Cell (2018) 173:1254-1264.e11. DOI 10.1016/j.cell.2018.03.018 · 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
8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
7E5E 1.95 Å, Crystal structure of GDP-bound GNAS in complex with the cyclic peptide inhibitor GD20
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 6AU6 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.