7MTR: Full-Length mGlu2

CryoEM Structure of Full-Length mGlu2 Bound to Ago-PAM ADX55164 and Glutamate. Determined by electron microscopy at 3.3 Å resolution. Released 7 Jul 2021.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 10,933
Mol. weight: 189.03 kDa
Ligands: ZQY, NAG, GLU
Released: 7 Jul 2021

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

Secondary structure: helices and β-sheets

7MTR contains 70 α-helices and 58 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: 34 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	10
β-strand	32-38	7	10
β-strand	41-43	3	11
β-strand	50-53	4	11
α-helix	59-73	15
β-strand	84-90	7	10
α-helix	95-101	7
α-helix	103-106	4
β-strand	136-141	6	10
α-helix	145-155	11
β-strand	162-164	3	10
α-helix	171-173	3
β-strand	182-183	2	10
α-helix	189-201	13
β-strand	204	1	12
β-strand	206-212	7	13
α-helix	217-229	13
β-strand	234-241	8	13
α-helix	247-258	12
β-strand	265-269	5	13
α-helix	272-285	14
β-strand	290-293	4	13
α-helix	308-311	4
β-strand	315-319	5	13
α-helix	325-331	7
α-helix	345-353	9
α-helix	378-399	22
α-helix	408-410	3
α-helix	415-417	3
α-helix	418-423	6
β-strand	428-429	2	14
α-helix	430	1
α-helix	433-434	2
β-strand	440-441	2	14
β-strand	453-460	8	13
β-strand	466-474	9	13
β-strand	478	1	13
α-helix	486-488	3
β-strand	498	1	12
α-helix	502-505	4
β-strand	508-512	5	15
α-helix	513	1
β-strand	520-524	5	15
α-helix	525-526	2
β-strand	529-533	5	16
β-strand	536-539	4	16
α-helix	540-541	2
β-strand	544-546	3	17
β-strand	553-555	3	17
β-strand	559	1	18
α-helix	566-591	26
α-helix	596-600	5
α-helix	604-624	21
α-helix	626-627	2
α-helix	631-659	29
α-helix	676-700	25
β-strand	705-707	3	19
β-strand	718	1	18
β-strand	719-721	3	19
α-helix	726-748	23
α-helix	760-774	15
α-helix	776-782	7
α-helix	787-790	4
α-helix	794-819	26

Chain B: 36 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	1
β-strand	32-38	7	1
β-strand	41-43	3	2
α-helix	44	1
β-strand	50-53	4	2
α-helix	54	1
α-helix	55-60	6
α-helix	61-72	12
β-strand	84-90	7	1
α-helix	95-106	12
β-strand	138-140	3	1
α-helix	145-158	14
β-strand	162-164	3	1
α-helix	171-173	3
β-strand	181-183	3	1
α-helix	191-201	11
β-strand	204	1	3
β-strand	206-212	7	4
α-helix	215-230	16
β-strand	234-241	8	4
α-helix	247-259	13
β-strand	265-269	5	4
α-helix	272-284	13
β-strand	290-293	4	4
α-helix	308-311	4
β-strand	315-319	5	4
α-helix	325-332	8
α-helix	345-353	9
α-helix	378-399	22
α-helix	415-417	3
α-helix	418-422	5
α-helix	423-425	3
β-strand	428-429	2	5
α-helix	430	1
β-strand	440-441	2	5
β-strand	453-460	8	4
β-strand	466-474	9	4
β-strand	478-480	3	4
α-helix	494-496	3
β-strand	498	1	3
α-helix	502-505	4
β-strand	508-511	4	6
β-strand	521-524	4	6
α-helix	525-526	2
β-strand	529-531	3	7
β-strand	537-539	3	7
β-strand	544-546	3	8
β-strand	553-555	3	8
α-helix	556-557	2
α-helix	566-591	26
α-helix	596-601	6
α-helix	605-623	19
α-helix	629-658	30
α-helix	678-700	23
β-strand	705-708	4	9
β-strand	718-721	4	9
α-helix	726-728	3
α-helix	729-748	20
α-helix	760-782	23
α-helix	783-785	3
α-helix	787-805	19
α-helix	806-810	5
α-helix	811-814	4
α-helix	815-819	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 2	A, B	protein	855	Homo sapiens	Q14416 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7MTR_1 Metabotropic glutamate receptor 2 (chains A, B)
AEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPH
LLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAIT
GVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAE
ILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRAL
LQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITI
ELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESK
IMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADT
HNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPA
SRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELP
QEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCY
CMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPA
SQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVL
LIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVS
VSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPT
VCNGREVVDSTTSSL

Ligands and cofactors

ID	Name	Formula	Copies
ZQY	2-methoxy-6-propyl-N-(2-{4-[(1H-tetrazol-5-yl)methoxy]phenyl}ethyl)thieno[2,3-d…	C20 H23 N7 O2 S	1
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
GLU	Glutamic acid	C5 H9 N O4	2

Primary citation

G-protein activation by a metabotropic glutamate receptor. Seven, A.B., Barros-Alvarez, X., de Lapeyriere, M. et al. Nature (2021) 595:450-454. DOI 10.1038/s41586-021-03680-3 · PubMed

Other PDB entries of the same protein (UniProt Q14416 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4XAQ 2.21 Å, mGluR2 ECD and mGluR3 ECD with ligands
4XAS 2.35 Å, mGluR2 ECD ligand complex
7EPE 2.5 Å, Crystal structure of mGlu2 bound to NAM563
5CNJ 2.65 Å, mGlur2 with glutamate analog
5CNI 2.69 Å, mGlu2 with Glutamate
7EPF 2.7 Å, Crystal structure of mGlu2 bound to NAM597
5KZN 2.8 Å, Metabotropic Glutamate Receptor
5KZQ 2.8 Å, Metabotropic Glutamate Receptor in complex with antagonist…
8JCU 2.8 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 (dimerization mode I)
8JD2 2.8 Å, Cryo-EM structure of G protein-free mGlu2-mGlu3 heterodimer in Acc state
8JCY 2.9 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and…
8JD4 2.9 Å, Cryo-EM structure of G protein-free mGlu2-mGlu4 heterodimer in Acc state

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