Cryo-EM structure of Mi3 fused with FKBP. Determined by electron microscopy at 3.68 Å resolution. Released 24 Apr 2024.
Explore 8JGA in 3D Show helices and sheets RCSB PDB PDBe
8JGA contains 11 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 | 12 | 1 | 1 |
| β-strand | 14-15 | 2 | 2 |
| α-helix | 21-34 | 14 | |
| β-strand | 38-42 | 5 | 2 |
| α-helix | 48-55 | 8 | |
| α-helix | 57-61 | 5 | |
| β-strand | 64-68 | 5 | 2 |
| α-helix | 73-81 | 9 | |
| β-strand | 86-88 | 3 | 2 |
| α-helix | 94-103 | 10 | |
| β-strand | 106-108 | 3 | 2 |
| β-strand | 110 | 1 | 3 |
| α-helix | 114-123 | 10 | |
| β-strand | 127-129 | 3 | 3 |
| α-helix | 133-136 | 4 | |
| α-helix | 138-144 | 7 | |
| β-strand | 152-154 | 3 | 3 |
| α-helix | 164-168 | 5 | |
| β-strand | 172 | 1 | 3 |
| β-strand | 175 | 1 | 1 |
| α-helix | 186-201 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase FKBP1A,2-dehydro-3-deoxyphosphogluconate… | A | protein | 344 | Homo sapiens, Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) | P62942 (AlphaFold model), Q9WXS1 (AlphaFold model) |
>8JGA_1 Peptidyl-prolyl cis-trans isomerase FKBP1A,2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase (chains A) MGSSHHHHHHGGSGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFK FMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE GGSGGSGGSGGSMKMEELFKKHKIVAVLRANSVEEAKKKALAVFLGGVHLIEITFTVPDA DTVIKELSFLKEMGAIIGAGTVTSVEQARKAVESGAEFIVSPHLDEEISQFAKEKGVFYM PGVMTPTELVKAMKLGHTILKLFPGEVVGPQFVKAMKGPFPNVKFVPTGGVNLDNVCEWF KAGVLAVGVGSALVKGTPVEVAEKAKAFVEKIRGCTEGSGEPEA
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 P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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