7WI8: Inactive mGlu3

Cryo-EM structure of inactive mGlu3 bound to LY341495. Determined by electron microscopy at 4.17 Å resolution. Released 16 Mar 2022.

Method
Electron microscopy
Resolution
4.17 Å
Organism
Homo sapiens
Chains
2
Atoms
9,268
Mol. weight
201.19 kDa
Ligands
Z99, NAG
Released
16 Mar 2022

Explore 7WI8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7WI8 contains 76 α-helices and 44 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.

Chains A and B: 38 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand33-3531
β-strand39-4351
α-helix66-7914
β-strand91-9551
α-helix102-11312
β-strand142-14651
α-helix151-1544
β-strand168-16921
β-strand18711
β-strand18912
α-helix192-1932
α-helix201-2033
α-helix205-2084
β-strand212-21763
α-helix223-2319
β-strand240-24673
β-strand272-27433
α-helix279-2813
α-helix282-2854
α-helix288-2914
β-strand297-29933
β-strand320-32563
α-helix331-3377
α-helix351-3599
α-helix390-3967
α-helix398-4058
α-helix407-4115
α-helix428-4347
β-strand44114
β-strand45314
β-strand46112
α-helix462-4643
β-strand466-47053
β-strand481-48663
β-strand490-49233
α-helix515-5173
β-strand52115
β-strand53015
β-strand538-53926
β-strand547-54826
α-helix553-5553
α-helix579-58810
α-helix590-5945
α-helix615-6184
α-helix621-63212
α-helix638-6458
α-helix648-6503
α-helix652-6554
α-helix657-66610
α-helix689-6946
α-helix696-6983
α-helix699-7079
α-helix734-7407
α-helix742-7476
α-helix750-7523
α-helix753-7575
α-helix772-78817
α-helix796-81015
α-helix811-8155
α-helix816-8194

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Metabotropic glutamate receptor 3A, Bprotein887Homo sapiensQ14832 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7WI8_1 Metabotropic glutamate receptor 3 (chains A, B)
MKTIIALSYIFCLVFADYKDDDDENLYFQGLGDHNFLRREIKIEGDLVLGGLFPINEKGT
GTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEF
VRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYA
STSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQ
EARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRAN
ASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFR
DFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLC
PNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQ
NVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICI
PCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTC
MVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSF
AICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAP
GTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIG
FTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQK
NVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL

Ligands and cofactors

IDNameFormulaCopies
Z992-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanineC20 H19 N O52
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Primary citation

Structural basis of the activation of metabotropic glutamate receptor 3. Fang, W., Yang, F., Xu, C. et al. Cell Res (2022) 32:695-698. DOI 10.1038/s41422-022-00623-z · PubMed

Other PDB entries of the same protein (UniProt Q14832 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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