5CNJ: MGlur2 with glutamate analog

mGlur2 with glutamate analog. Determined by X-ray diffraction at 2.65 Å resolution. Released 9 Sept 2015.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 2
Atoms: 7,184
Mol. weight: 112.13 kDa
Ligands: NAG, 52Q
Released: 9 Sept 2015

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

Secondary structure: helices and β-sheets

5CNJ contains 48 α-helices and 38 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: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	1
β-strand	32-38	7	1
β-strand	41-43	3	2
β-strand	50-53	4	2
α-helix	55-60	6
α-helix	61-72	12
β-strand	84-90	7	1
α-helix	95-101	7
α-helix	102-105	4
α-helix	134-135	2
β-strand	136-141	6	1
α-helix	145-157	13
β-strand	162-164	3	1
α-helix	170-173	4
β-strand	181-183	3	1
α-helix	188-201	14
β-strand	206-212	7	3
α-helix	217-230	14
β-strand	234-241	8	3
α-helix	247-258	12
β-strand	265-269	5	3
α-helix	272-284	13
β-strand	290-293	4	3
α-helix	301-304	4
α-helix	308-311	4
β-strand	315-319	5	3
α-helix	325-332	8
α-helix	345-352	8
α-helix	357-359	3
α-helix	378-399	22
α-helix	408-410	3
α-helix	415-417	3
α-helix	418-422	5
α-helix	423-425	3
β-strand	427-429	3	4
α-helix	430	1
β-strand	440-442	3	4
β-strand	452-460	9	3
β-strand	466-475	10	3
β-strand	478-480	3	3
α-helix	482-484	3

Chain B: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	5
β-strand	32-38	7	5
β-strand	41-43	3	6
β-strand	50-53	4	6
α-helix	55-60	6
α-helix	61-73	13
β-strand	84-90	7	5
α-helix	95-102	8
α-helix	103-106	4
β-strand	138-141	4	5
α-helix	145-155	11
α-helix	156-158	3
β-strand	162-164	3	5
α-helix	171-173	3
β-strand	181-183	3	5
α-helix	186-187	2
α-helix	188-201	14
β-strand	206-211	6	7
β-strand	212	1	8
α-helix	215-229	15
β-strand	234-238	5	7
β-strand	241	1	8
α-helix	247-258	12
β-strand	265-269	5	7
α-helix	272-284	13
β-strand	290-293	4	7
α-helix	301-304	4
α-helix	308-311	4
β-strand	315-319	5	7
α-helix	325-332	8
α-helix	345-352	8
α-helix	367-369	3
α-helix	378-399	22
α-helix	408-410	3
α-helix	415-417	3
α-helix	418-422	5
α-helix	423-425	3
β-strand	427-429	3	9
α-helix	430	1
β-strand	440-442	3	9
α-helix	448-450	3
β-strand	453-460	8	7
α-helix	462-464	3
β-strand	466-474	9	7
β-strand	478-480	3	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 2	A, B	protein	503	Homo sapiens	Q14416 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5CNJ_1 Metabotropic glutamate receptor 2 (chains A, B)
MALGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRG
IQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSR
HICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRY
DYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNISVATS
EKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWG
ALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFR
QRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRL
YKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGL
TLDTSLIPWASPSAGEGHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
52Q	(1R,2S,4R,5R,6R)-2-amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-…	C10 H12 N4 O4 S	2

Primary citation

Synthesis and Pharmacological Characterization of C4-(Thiotriazolyl)-substituted-2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylates. Identification of (1R,2S,4R,5R,6R)-2-Amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-2,6-dicarboxylic Acid (LY2812223), a Highly Potent, Functionally…. Monn, J.A., Prieto, L., Taboada, L. et al. J Med Chem (2015) 58:7526-7548. DOI 10.1021/acs.jmedchem.5b01124 · 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
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
8JCW 3.0 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 and NAM563…

Browse structure collections

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