5DSG: M4 muscarinic acetylcholine receptor

Structure of the M4 muscarinic acetylcholine receptor (M4-mT4L) bound to tiotropium. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Mar 2016.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Homo sapiens, Enterobacteria phage T4
Chains: 2
Atoms: 6,516
Mol. weight: 100.7 kDa
Ligands: PG6, OLC, EDT, OLA
Released: 16 Mar 2016

Explore 5DSG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5DSG contains 51 α-helices and 0 β-strands across 2 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: 25 helices, 0 β-strands

Element	Residues	Length
α-helix	24-25	2
α-helix	26-59	34
α-helix	61-63	3
α-helix	66-80	15
α-helix	81-85	5
α-helix	86-95	10
α-helix	101-135	35
α-helix	141-143	3
α-helix	146-169	24
α-helix	171-175	5
α-helix	188-190	3
α-helix	193-200	8
α-helix	201-205	5
α-helix	206-220	15
α-helix	226-1010	10
α-helix	1021-1037	17
α-helix	1041-1046	6
α-helix	1050-1069	20
α-helix	1072-1079	8
α-helix	1083-1090	8
α-helix	1094-1098	5
α-helix	1100-1112	13
α-helix	397-422	26
α-helix	432-456	25
α-helix	458-468	11

Chain B: 26 helices, 0 β-strands

Element	Residues	Length
α-helix	27-59	33
α-helix	61-63	3
α-helix	66-80	15
α-helix	81-85	5
α-helix	86-95	10
α-helix	101-135	35
α-helix	146-169	24
α-helix	171-175	5
α-helix	188-190	3
α-helix	193-200	8
α-helix	201-205	5
α-helix	206-221	16
α-helix	1003-1009	7
α-helix	1021-1037	17
α-helix	1041-1046	6
α-helix	1050-1063	14
α-helix	1065-1069	5
α-helix	1072-1079	8
α-helix	1083-1091	9
α-helix	1095-1098	4
α-helix	1100-1112	13
α-helix	391-392	2
α-helix	393-422	30
α-helix	432-441	10
α-helix	444-456	13
α-helix	459-468	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Muscarinic acetylcholine receptor M4,Endolysin,Endolysin,Muscarinic acetylcholine receptor M4	A, B	protein	422	Homo sapiens, Enterobacteria phage T4	P00720, P08173 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5DSG_1 Muscarinic acetylcholine receptor M4,Endolysin,Endolysin,Muscarinic acetylcholine receptor M4 (chains A, B)
GPSSHNRYETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADL
IIGAFSMNLYTVYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLT
YPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGT
AIAAFYLPVVIMTVLYIHISLASRSRVNIFEMLRIDEGGGSGGDEAEKLFNQDVDAAVRG
ILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSR
WYNQTPNRAKRVITTFRTGTWDAYQMAARERKVTRTIFAILLAFILTWTPYNVMVLVNTF
CQSCIPDTVWSIGYWLCYVNSTINPACYALCNATFKKTFRHLLLCQYRNIGTARHHHHHH
HH

Ligands and cofactors

ID	Name	Formula	Copies
PG6	1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane	C12 H26 O6	1
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	5
EDT	{[-(bis-carboxymethyl-amino)-ethyl]-carboxymethyl-amino}-acetic acid	C10 H16 N2 O8	1
OLA	Oleic acid	C18 H34 O2	5
0HK	(1R,2R,4S,5S,7S)-7-{[hydroxy(dithiophen-2-yl)acetyl]oxy}-9,9-dimethyl-3-oxa-9-a…	C19 H22 N O4 S2	2

Water and common crystallization additives (P6G) are not listed.

Primary citation

Crystal structures of the M1 and M4 muscarinic acetylcholine receptors. Thal, D.M., Sun, B., Feng, D. et al. Nature (2016) 531:335-340. DOI 10.1038/nature17188 · PubMed

Other PDB entries of the same protein (UniProt P00720), best resolution first:

2O7A 0.84 Å, T4 lysozyme C-terminal fragment
5JDT 1.0 Å, Structure of Spin-labelled T4 lysozyme mutant L118C-R1 at 100K
7LOE 1.01 Å, T4 lysozyme mutant L99A in complex with 1-fluoranylnaphthalene
7LOD 1.02 Å, T4 lysozyme mutant L99A in complex with 1-fluoranyl-4-iodanyl-benzene
7LX8 1.03 Å, T4 lysozyme mutant L99A
5XPF 1.04 Å, High-resolution X-ray structure of the T26H mutant of T4 lysozyme
6BG3 1.05 Å, Structure of (3S,4S)-1-benzyl-4-(3-(3-(trifluoromethyl)phenyl)ureido)piperidin-3-yl…
7LOF 1.05 Å, T4 lysozyme mutant L99A in complex with 2-butylthiophene
7LX6 1.05 Å, T4 lysozyme mutant L99A
7LX7 1.05 Å, T4 lysozyme mutant L99A
1SWY 1.06 Å, Use of a Halide Binding Site to Bypass the 1000-atom Limit to Ab initio Structure…
1SWZ 1.06 Å, Use of an ion-binding site to bypass the 1000-atom limit to ab initio structure…

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