5CNM: MGluR3

mGluR3 complexed with glutamate analog. Determined by X-ray diffraction at 2.84 Å resolution. Released 9 Sept 2015.

Method
X-ray diffraction
Resolution
2.84 Å
Organism
Homo sapiens
Chains
1
Atoms
3,494
Mol. weight
59.25 kDa
Ligands
52Q, MG
Released
9 Sept 2015

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

Secondary structure: helices and β-sheets

5CNM contains 25 α-helices and 22 β-strands across 1 chain. 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: 25 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand33-3531
β-strand39-4571
β-strand48-5032
α-helix51-522
β-strand57-6042
α-helix62-676
α-helix68-7912
β-strand91-9771
α-helix102-11615
β-strand142-14651
α-helix151-16313
β-strand168-17031
α-helix176-1794
β-strand187-18931
α-helix192-1932
α-helix196-20712
β-strand212-21873
α-helix221-23616
β-strand240-24783
α-helix253-26412
β-strand271-27553
α-helix278-29013
β-strand296-29943
α-helix307-3104
α-helix314-3174
β-strand321-32553
α-helix331-3388
α-helix351-3599
β-strand36214
α-helix3711
β-strand37214
α-helix373-3742
α-helix390-41122
α-helix420-4234
α-helix427-4293
α-helix430-4345
α-helix435-4373
β-strand440-44125
α-helix450-4523
β-strand453-45425
β-strand45616
α-helix4611
β-strand46216
α-helix4631
β-strand466-47163
β-strand480-48673
β-strand490-49233

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Metabotropic glutamate receptor 3Aprotein517Homo sapiensQ14832 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5CNM_1 Metabotropic glutamate receptor 3 (chains A)
MALKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECG
RINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLT
KVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKL
SDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRN
ISIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWV
ASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQK
FQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKL
CDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKY
SYLKVGHWAETLSLDVNSIHWSRNSVPTSEGHHHHHH

Ligands and cofactors

IDNameFormulaCopies
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 S1
MGMagnesium ionMg1

Water and common crystallization additives (CL, SO4) 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:

Browse structure collections

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