mGluR2 ECD and mGluR3 ECD complex with ligands. Determined by X-ray diffraction at 2.26 Å resolution. Released 11 Feb 2015.
Explore 4XAR in 3D Show helices and sheets RCSB PDB PDBe
4XAR contains 25 α-helices and 20 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.
| 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 | 102-109 | 8 | |
| α-helix | 110-112 | 3 | |
| α-helix | 114-116 | 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 | 307-310 | 4 | |
| β-strand | 321-325 | 5 | 3 |
| α-helix | 331-338 | 8 | |
| α-helix | 351-358 | 8 | |
| β-strand | 362 | 1 | 4 |
| β-strand | 372 | 1 | 4 |
| α-helix | 373-374 | 2 | |
| α-helix | 390-411 | 22 | |
| α-helix | 420-422 | 3 | |
| α-helix | 427-429 | 3 | |
| α-helix | 430-435 | 6 | |
| β-strand | 438-440 | 3 | 5 |
| β-strand | 453-455 | 3 | 5 |
| β-strand | 465-473 | 9 | 3 |
| β-strand | 478-487 | 10 | 3 |
| β-strand | 489-492 | 4 | 3 |
| α-helix | 494-496 | 3 | |
| α-helix | 503-505 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 3 | A | protein | 517 | Homo sapiens | Q14832 (AlphaFold model) |
>4XAR_1 Metabotropic glutamate receptor 3 (chains A) MALKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECG RINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLT KVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKL SDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRN ISIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWV ASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQK FQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKL CDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKY SYLKVGHWAETLSLDVNSIHWSRNSVPTSEGHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 40F | (1S,2S,5R,6S)-2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylic acid | C8 H11 N O4 | 1 |
Water and common crystallization additives (IOD) are not listed.
Synthesis and Pharmacological Characterization of C4-Disubstituted Analogs of 1S,2S,5R,6S-2-Aminobicyclo[3.1.0]hexane-2,6-dicarboxylate: Identification of a Potent, Selective Metabotropic Glutamate Receptor Agonist and Determination of Agonist-Bound Human mGlu2 and mGlu3 Amino Terminal Domain…. Monn, J.A., Prieto, L., Taboada, L. et al. J Med Chem (2015) 58:1776-1794. DOI 10.1021/jm501612y · PubMed
Other PDB entries of the same protein (UniProt Q14832 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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