Crystal structure of MBPapo-Tim21 fusion protein with a 16-residue helical linker. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Sept 2019.
Explore 6K7D in 3D Show helices and sheets RCSB PDB PDBe
6K7D contains 28 α-helices and 32 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 | 3-4 | 2 | |
| β-strand | 8-11 | 4 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 36-39 | 4 | 1 |
| α-helix | 44-52 | 9 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 68-73 | 6 | |
| β-strand | 77 | 1 | 2 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-95 | 4 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 115-119 | 5 | 5 |
| β-strand | 129 | 1 | 6 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-142 | 10 | |
| β-strand | 146-148 | 3 | 5 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 7 |
| β-strand | 176-183 | 8 | 7 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-218 | 8 | |
| β-strand | 223-228 | 6 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-239 | 7 | |
| β-strand | 243-246 | 4 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 6 |
| β-strand | 251 | 1 | 8 |
| β-strand | 254 | 1 | 8 |
| β-strand | 259-260 | 2 | 9 |
| β-strand | 261-267 | 7 | 1 |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 1 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 9 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-352 | 16 | |
| α-helix | 358-398 | 41 | |
| α-helix | 401-406 | 6 | |
| β-strand | 412 | 1 | 10 |
| β-strand | 415 | 1 | 10 |
| β-strand | 420-422 | 3 | 11 |
| α-helix | 423-425 | 3 | |
| β-strand | 439-443 | 5 | 11 |
| α-helix | 448 | 1 | |
| β-strand | 449-458 | 10 | 11 |
| β-strand | 463-471 | 9 | 11 |
| α-helix | 479 | 1 | |
| β-strand | 480-487 | 8 | 11 |
| β-strand | 494-497 | 4 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Mitochondrial import inner membrane translocase… | A | protein | 506 | Escherichia coli (strain K12), Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P0AEX9 (AlphaFold model), P53220 (AlphaFold model) |
>6K7D_1 Maltose/maltodextrin-binding periplasmic protein,Mitochondrial import inner membrane translocase subunit TIM21 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELVKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTRIEAAAKEAAAKEAAAKADTQLFNRAVSMVEKNKDIRSLLQCDDGITGKERLK AYGELITNDKWTRNRPIVSTKKLDKEGRTHHYMRFHVESKKKIALVHLEAKESKQNYQPD FINMYVDVPGEKRYYLIKLEHHHHHH
Crystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study. Bala, S., Shinya, S., Srivastava, A. et al. Biochim Biophys Acta Gen Subj (2020) 1864:129418-129418. DOI 10.1016/j.bbagen.2019.129418 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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