Crystal structure of the MBP-MCL1 complex with highly selective and potent inhibitor of MCL1. Determined by X-ray diffraction at 2.2 Å resolution. Released 26 Oct 2016.
Explore 5LOF in 3D Show helices and sheets RCSB PDB PDBe
5LOF contains 32 α-helices and 25 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 | -194--193 | 2 | |
| β-strand | -190--186 | 5 | 1 |
| α-helix | -179--165 | 15 | |
| β-strand | -162--158 | 5 | 1 |
| α-helix | -153--145 | 9 | |
| β-strand | -137--133 | 5 | 1 |
| α-helix | -132--130 | 3 | |
| α-helix | -129--124 | 6 | |
| β-strand | -120 | 1 | 2 |
| α-helix | -119--117 | 3 | |
| α-helix | -113--110 | 4 | |
| β-strand | -107 | 1 | 3 |
| α-helix | -105--100 | 6 | |
| β-strand | -98--97 | 2 | 4 |
| β-strand | -94--93 | 2 | 4 |
| β-strand | -90--85 | 6 | 1 |
| β-strand | -82--78 | 5 | 5 |
| β-strand | -68 | 1 | 6 |
| α-helix | -64--56 | 9 | |
| β-strand | -51 | 1 | 7 |
| α-helix | -42--33 | 10 | |
| β-strand | -29--26 | 4 | 8 |
| β-strand | -19--14 | 6 | 8 |
| α-helix | -10-4 | 15 | |
| α-helix | 14-22 | 9 | |
| β-strand | 26 | 1 | 7 |
| β-strand | 28-31 | 4 | 5 |
| α-helix | 33-35 | 3 | |
| α-helix | 36-41 | 6 | |
| β-strand | 46-49 | 4 | 5 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 6 |
| β-strand | 54 | 1 | 9 |
| β-strand | 57 | 1 | 9 |
| α-helix | 61 | 1 | |
| β-strand | 62-63 | 2 | 10 |
| β-strand | 64-70 | 7 | 1 |
| β-strand | 71 | 1 | 2 |
| α-helix | 77-83 | 7 | |
| α-helix | 84-88 | 5 | |
| α-helix | 91-100 | 10 | |
| β-strand | 105-106 | 2 | 1 |
| β-strand | 108 | 1 | 3 |
| α-helix | 109-115 | 7 | |
| α-helix | 119-130 | 12 | |
| β-strand | 132-133 | 2 | 10 |
| α-helix | 134-135 | 2 | |
| α-helix | 140-156 | 17 | |
| α-helix | 161-191 | 31 | |
| α-helix | 203-223 | 21 | |
| α-helix | 225-234 | 10 | |
| α-helix | 240-255 | 16 | |
| α-helix | 261-280 | 20 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-301 | 15 | |
| α-helix | 303-308 | 6 | |
| α-helix | 311-318 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein,Induced myeloid leukemia cell differentiation protein Mcl-1 | A | protein | 518 | Escherichia coli O157:H7, Homo sapiens | P0AEY0 (AlphaFold model), Q07820 (AlphaFold model) |
>5LOF_1 Maltose-binding periplasmic protein,Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTGSELYRQSLEIISRYLREQATGAADTAPMGASGATSRKALETLRRVGDGVQRN HETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQ ESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 70R | (2~{R})-2-[5-[3-chloranyl-2-methyl-4-[2-(4-methylpiperazin-1-yl)ethoxy]phenyl]-… | C39 H37 Cl F4 N6 O6 S | 1 |
The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models. Kotschy, A., Szlavik, Z., Murray, J. et al. Nature (2016) 538:477-482. DOI 10.1038/nature19830 · PubMed
Other PDB entries of the same protein (UniProt P0AEY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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