Cryo-EM structure of Mi3 fused with LOV2. Determined by electron microscopy at 3.44 Å resolution. Released 24 Apr 2024.
Explore 8JGC in 3D Show helices and sheets RCSB PDB PDBe
8JGC contains 7 α-helices and 11 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 | 3-10 | 8 | |
| β-strand | 14 | 1 | 1 |
| β-strand | 15-16 | 2 | 2 |
| α-helix | 23-34 | 12 | |
| β-strand | 38-42 | 5 | 2 |
| α-helix | 48-61 | 14 | |
| β-strand | 64-68 | 5 | 2 |
| α-helix | 73-81 | 9 | |
| β-strand | 86-88 | 3 | 3 |
| α-helix | 94-103 | 10 | |
| β-strand | 106-108 | 3 | 3 |
| β-strand | 110 | 1 | 4 |
| α-helix | 114-121 | 8 | |
| β-strand | 129 | 1 | 4 |
| β-strand | 153 | 1 | 5 |
| β-strand | 172 | 1 | 5 |
| β-strand | 177 | 1 | 1 |
| α-helix | 186-202 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| LOV domain-containing protein,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate… | A | protein | 378 | Aegilops tauschii subsp. strangulata, Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) | Q9WXS1 (AlphaFold model) |
>8JGC_1 LOV domain-containing protein,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase (chains A) MGSSEFLATTLERIEKNFVITDPRLPDNPIIFASDSFLQLTEYSREEILGRNCRFLQGPE TDRATVRKIRDAIDNQTEVTVQLINYTKSGKKFWNVFHLQPMRDYKGDVQYFIGVQLDGT ERLHGAAEREAVCLIKKTAFQIAEAANDENYFGGSGGSGGSGGSMKMEELFKKHKIVAVL RANSVEEAKKKALAVFLGGVHLIEITFTVPDADTVIKELSFLKEMGAIIGAGTVTSVEQA RKAVESGAEFIVSPHLDEEISQFAKEKGVFYMPGVMTPTELVKAMKLGHTILKLFPGEVV GPQFVKAMKGPFPNVKFVPTGGVNLDNVCEWFKAGVLAVGVGSALVKGTPVEVAEKAKAF VEKIRGCTEGSGHHHHHH
Dynamic Metabolons Using Stimuli-Responsive Protein Cages. Kang, W., Ma, X., Zhang, H. et al. J Am Chem Soc (2024) 146:6686-6696. DOI 10.1021/jacs.3c12876 · PubMed
Other PDB entries of the same protein (UniProt Q9WXS1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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