8JD1: MGlu2-mGlu3 heterodimer in Rco state

Cryo-EM structure of mGlu2-mGlu3 heterodimer in Rco state. Determined by electron microscopy at 3.7 Å resolution. Released 21 Jun 2023.

Method: Electron microscopy
Resolution: 3.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 10,766
Mol. weight: 225.11 kDa
Ligands: GLU, CLR
Released: 21 Jun 2023

Explore 8JD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8JD1 contains 60 α-helices and 52 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 2: 31 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	1
β-strand	32	1	2
β-strand	35-37	3	1
α-helix	55-59	5
α-helix	60-74	15
β-strand	84	1	2
β-strand	86-88	3	1
α-helix	95-107	13
α-helix	134-136	3
β-strand	139-141	3	1
α-helix	145-155	11
β-strand	162-164	3	1
α-helix	170-172	3
β-strand	181-183	3	1
α-helix	186-187	2
α-helix	191-201	11
β-strand	204	1	3
β-strand	206-210	5	4
α-helix	215-228	14
β-strand	234-239	6	4
α-helix	247-257	11
β-strand	265-268	4	4
α-helix	272-285	14
β-strand	290-293	4	4
α-helix	295-297	3
α-helix	301-304	4
β-strand	316	1	4
β-strand	317-319	3	5
α-helix	326-331	6
α-helix	345-353	9
α-helix	357-359	3
α-helix	378-399	22
α-helix	408-410	3
α-helix	415-422	8
α-helix	428-430	3
β-strand	448	1	1
β-strand	453-459	7	5
β-strand	467-474	8	5
β-strand	478	1	5
α-helix	482-484	3
β-strand	498	1	3
β-strand	531	1	6
β-strand	537	1	6
β-strand	560	1	7
α-helix	569-592	24
α-helix	597-599	3
α-helix	603-621	19
α-helix	629-659	31
α-helix	676-701	26
β-strand	718	1	7
α-helix	722-749	28
α-helix	757-778	22
α-helix	779-783	5
α-helix	789-809	21
α-helix	811-816	6

Chain 3: 29 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	8
β-strand	48	1	9
β-strand	60	1	9
α-helix	66-80	15
β-strand	91-97	7	8
α-helix	102-109	8
α-helix	112-114	3
β-strand	142-146	5	8
α-helix	151-164	14
β-strand	168-170	3	8
β-strand	187-189	3	8
α-helix	196-207	12
β-strand	212-216	5	10
β-strand	218	1	11
α-helix	221-236	16
β-strand	240-244	5	10
β-strand	247	1	11
α-helix	256-264	9
β-strand	271-274	4	10
α-helix	278-291	14
β-strand	296-299	4	10
β-strand	321-325	5	10
α-helix	328-330	3
α-helix	331-338	8
α-helix	351-358	8
β-strand	362	1	12
β-strand	372	1	12
α-helix	381-383	3
α-helix	388-390	3
α-helix	391-411	21
α-helix	420-422	3
α-helix	428-429	2
α-helix	430-434	5
α-helix	435-437	3
β-strand	440	1	13
β-strand	454	1	13
β-strand	466-471	6	10
β-strand	474	1	14
β-strand	477	1	14
β-strand	480-486	7	10
α-helix	503-505	3
β-strand	539	1	15
β-strand	547	1	15
β-strand	554-555	2	16
β-strand	562-563	2	16
α-helix	564-567	4
α-helix	576-578	3
α-helix	579-601	23
α-helix	614-632	19
α-helix	638-663	26
α-helix	683-704	22
α-helix	708-710	3
β-strand	716-718	3	17
β-strand	727-729	3	17
α-helix	734-753	20
α-helix	762-791	30
α-helix	800-828	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 2,Peptidyl-prolyl cis-trans isomerase FKBP1A	2	protein	993	Homo sapiens	P62942 (AlphaFold model), Q14416 (AlphaFold model)
Metabotropic glutamate receptor 3,Serine/threonine-protein kinase mTOR	3	protein	993	Homo sapiens	A0A8V8TRG9, Q14832 (AlphaFold model)

Sequence of entity 1 (2), FASTA

>8JD1_1 Metabotropic glutamate receptor 2,Peptidyl-prolyl cis-trans isomerase FKBP1A (chains 2)
DYKDDDDGAPEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFA
LDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYAT
HGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPD
FFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRA
AFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSE
GAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLR
AVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKF
DAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWA
SPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNA
SLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYI
LLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGA
QRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASM
LGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYR
VQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQ
GSGSQFVPTVCNGREVVDSTTSSLLEVLFQGPGVQVETISPGDGRTFPKRGQTCVVHYTG
MLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHP
GIIPPHATLVFDVELLKLEFAAAHHHHHHHHHH

Sequence of entity 2 (3), FASTA

>8JD1_2 Metabotropic glutamate receptor 3,Serine/threonine-protein kinase mTOR (chains 3)
DYKDDDDKGAPWSHPQFEKGSGSWSHPQFEKLGDHNFLRREIKIEGDLVLGGLFPINEKG
TGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLE
FVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISY
ASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFE
QEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRA
NASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWF
RDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTL
CPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNF
QNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWIC
IPCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCT
CMVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSS
FAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEA
PGTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFI
GFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQ
KNVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSLLEVLFQGPAILW
HEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQE
WCRKYMKSGNVKDLTQAWDLYYHVFRRISKQEF

Ligands and cofactors

ID	Name	Formula	Copies
GLU	Glutamic acid	C5 H9 N O4	2
CLR	Cholesterol	C27 H46 O	7

Primary citation

Structural insights into dimerization and activation of the mGlu2-mGlu3 and mGlu2-mGlu4 heterodimers. Wang, X., Wang, M., Xu, T. et al. Cell Res (2023) 33:762-774. DOI 10.1038/s41422-023-00830-2 · PubMed

Other PDB entries of the same protein (UniProt P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2PPN 0.92 Å, Crystal structure of FKBP12
2PPP 0.94 Å, Crystal structure of E60Q mutant of FKBP12
6YF3 1.0 Å, FKBP12 in complex with the BMP potentiator compound 10 at 1.00A resolution
6YF2 1.03 Å, FKBP12 in complex with the BMP potentiator compound 6 at 1.03A resolution
8X6P 1.05 Å, Isomerase Protein
6YF1 1.12 Å, FKBP12 in complex with the BMP potentiator compound 8 at 1.12A resolution
8CHM 1.12 Å, Human FKBP12 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)-3-(pyridin-…
4N19 1.2 Å, Structural basis of conformational transitions in the active site and 80 s loop in the…
8PDF 1.2 Å, FKBP12 in complex with PROTAC 6a2
9LYG 1.26 Å, Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201
2PPO 1.29 Å, Crystal structure of E60A mutant of FKBP12
7U8D 1.39 Å, FKBP12 mutant V55G bound to Rapa*-3Z

Browse structure collections

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