Cryo-EM structure of apo-state MrgD-Gi complex (local). Determined by electron microscopy at 3.1 Å resolution. Released 20 Jul 2022.
Explore 7Y13 in 3D Show helices and sheets RCSB PDB PDBe
7Y13 contains 14 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 23-52 | 30 | |
| α-helix | 62-85 | 24 | |
| α-helix | 97-128 | 32 | |
| α-helix | 130-135 | 6 | |
| α-helix | 141-164 | 24 | |
| α-helix | 173-185 | 13 | |
| α-helix | 186-190 | 5 | |
| α-helix | 191-204 | 14 | |
| α-helix | 205-209 | 5 | |
| α-helix | 217-229 | 13 | |
| α-helix | 230-234 | 5 | |
| α-helix | 235-244 | 10 | |
| α-helix | 254-273 | 20 | |
| α-helix | 274-278 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Soluble cytochrome b562,Mas-related G-protein coupled receptor member D | R | protein | 446 | Escherichia coli, Homo sapiens | P0ABE7 (AlphaFold model), Q8TDS7 (AlphaFold model) |
>7Y13_1 Soluble cytochrome b562,Mas-related G-protein coupled receptor member D (chains R) MKTIIALSYIFCLVFADYKDDDDKADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAA ALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKT TRNAYIQKYLNSSGTVESALNYSRGSTVHTAYLVLSSLAMFTCLCGMAGNSMVIWLLGFR MHRNPFCIYILNLAAADLLFLFSMASTLSLETQPLVNTTDKVHELMKRLMYFAYTVGLSL LTAISTQRCLSVLFPIWFKCHRPRHLSAWVCGLLWTLCLLMNGLTSSFCSKFLKFNEDRC FRVDMVQAALIMGVLTPVMTLSSLTLFVWVRRSSQQWRRQPTRLFVVVLASVLVFLICSL PLSIYWFVLYWLSLPPEMQVLCFSLSRLSSSVSSSANPVIYFLVGSRRSHRLPTRSLGTV LQQALREEPELEGGETPTVGTNEMGA
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLM | Palmitic acid | C16 H32 O2 | 7 |
Structural insight into the activation mechanism of MrgD with heterotrimeric Gi-protein revealed by cryo-EM. Suzuki, S., Iida, M., Hiroaki, Y. et al. Commun Biol (2022) 5:707-707. DOI 10.1038/s42003-022-03668-3 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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