5CNK: Mglur3 with glutamate

mglur3 with glutamate. Determined by X-ray diffraction at 3.15 Å resolution. Released 9 Sept 2015.

Method: X-ray diffraction
Resolution: 3.15 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,563
Mol. weight: 177.75 kDa
Ligands: GLU
Released: 9 Sept 2015

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

Secondary structure: helices and β-sheets

5CNK contains 64 α-helices and 58 β-strands across 3 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, 20 β-strands

Element	Residues	Length	Sheet
β-strand	33-35	3	1
β-strand	39-45	7	1
β-strand	48-50	3	2
α-helix	51	1
β-strand	57-60	4	2
α-helix	62-66	5
α-helix	67-79	13
α-helix	90	1
β-strand	91-97	7	1
α-helix	102-114	13
α-helix	139-141	3
β-strand	144-146	3	1
α-helix	151-161	11
α-helix	162-164	3
β-strand	168-170	3	1
α-helix	176-179	4
β-strand	187-189	3	1
α-helix	194-207	14
β-strand	212-218	7	3
α-helix	221-236	16
β-strand	240-247	8	3
α-helix	253-255	3
α-helix	256-264	9
β-strand	271-275	5	3
α-helix	278-290	13
β-strand	296-299	4	3
α-helix	307-309	3
β-strand	321-325	5	3
α-helix	331-338	8
α-helix	351-359	9
β-strand	362	1	4
β-strand	372	1	4
α-helix	373-374	2
α-helix	390-411	22
α-helix	420-423	4
α-helix	427-429	3
α-helix	430-435	6
β-strand	438-440	3	5
β-strand	453-455	3	5
β-strand	466-472	7	3
β-strand	479-486	8	3
β-strand	490-492	3	3
α-helix	494-496	3

Chain B: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	33-35	3	6
β-strand	39-45	7	6
β-strand	48-50	3	7
α-helix	51-52	2
β-strand	57-60	4	7
α-helix	62-67	6
α-helix	68-79	12
α-helix	90	1
β-strand	91-97	7	6
α-helix	102-113	12
β-strand	142-147	6	6
α-helix	151-161	11
α-helix	162-164	3
β-strand	168-170	3	6
α-helix	176-179	4
β-strand	187-189	3	6
α-helix	194-207	14
β-strand	212-217	6	8
α-helix	221-235	15
β-strand	240-246	7	8
α-helix	254-264	11
β-strand	271-275	5	8
α-helix	278-290	13
β-strand	296-299	4	8
α-helix	307-310	4
β-strand	321-325	5	8
α-helix	331-338	8
α-helix	351-359	9
α-helix	372-374	3
α-helix	390-411	22
α-helix	420-423	4
α-helix	427-429	3
α-helix	430-434	5
β-strand	439-440	2	9
β-strand	453-454	2	9
β-strand	466-472	7	8
β-strand	479-486	8	8
β-strand	490-492	3	8

Chain C: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	33-35	3	10
β-strand	39-45	7	10
β-strand	48-50	3	11
α-helix	51	1
β-strand	57-60	4	11
α-helix	62-66	5
α-helix	67-79	13
α-helix	90	1
β-strand	91-97	7	10
α-helix	102-115	14
α-helix	140-141	2
β-strand	142-147	6	10
α-helix	151-161	11
α-helix	162-164	3
β-strand	168-170	3	10
α-helix	176-179	4
β-strand	187-189	3	10
α-helix	194-207	14
β-strand	212-218	7	12
α-helix	221-236	16
β-strand	240-247	8	12
α-helix	255-264	10
β-strand	271-275	5	12
α-helix	278-290	13
β-strand	296-299	4	12
α-helix	307-310	4
β-strand	321-325	5	12
α-helix	331-338	8
α-helix	351-359	9
β-strand	362	1	13
β-strand	372	1	13
α-helix	373-374	2
α-helix	390-411	22
α-helix	420-423	4
α-helix	427-429	3
α-helix	430-435	6
β-strand	438-440	3	14
β-strand	453-455	3	14
β-strand	466-472	7	12
β-strand	479-486	8	12
β-strand	490-492	3	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 3	A, B, C	protein	517	Homo sapiens	Q14832 (AlphaFold model)

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

>5CNK_1 Metabotropic glutamate receptor 3 (chains A, B, C)
MALKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECG
RINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLT
KVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKL
SDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRN
ISIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWV
ASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQK
FQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKL
CDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKY
SYLKVGHWAETLSLDVNSIHWSRNSVPTSEGHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
GLU	Glutamic acid	C5 H9 N O4	1

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

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 Q14832 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SM9 2.26 Å, Crystal Structure of Metabotropic glutamate receptor 3 precursor in presence of LY341495…
4XAR 2.26 Å, mGluR2 ECD and mGluR3 ECD complex with ligands
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
6B7H 2.82 Å, Structure of mGluR3 with an agonist
5CNM 2.84 Å, mGluR3 complexed with glutamate analog
8JCY 2.9 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and…
8JCW 3.0 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 and NAM563…
8JCX 3.0 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495 and NAM563…
8JCZ 3.0 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of LY341495, NAM563, and…
8JD0 3.3 Å, Cryo-EM structure of mGlu2-mGlu3 heterodimer in presence of NAM563
8JD3 3.3 Å, Cryo-EM structure of Gi1-bound mGlu2-mGlu3 heterodimer

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