STRUCTURE OF MBP-MCL1 BOUND TO ligand 2 AT 1.55A. Determined by X-ray diffraction at 1.55 Å resolution. Released 6 May 2015.
Explore 4WMU in 3D Show helices and sheets RCSB PDB PDBe
4WMU contains 34 α-helices and 24 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 | -193 | 1 | |
| β-strand | -189--186 | 4 | 1 |
| α-helix | -179--165 | 15 | |
| β-strand | -161--158 | 4 | 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 | -67--65 | 3 | |
| α-helix | -64--56 | 9 | |
| β-strand | -51--49 | 3 | 5 |
| α-helix | -42--33 | 10 | |
| β-strand | -29--25 | 5 | 7 |
| β-strand | -20--14 | 7 | 7 |
| α-helix | -10-4 | 15 | |
| α-helix | 14-22 | 9 | |
| β-strand | 26-31 | 6 | 5 |
| α-helix | 33-35 | 3 | |
| α-helix | 36-42 | 7 | |
| β-strand | 46-49 | 4 | 5 |
| α-helix | 50-52 | 3 | |
| β-strand | 53 | 1 | 6 |
| β-strand | 54 | 1 | 8 |
| β-strand | 57 | 1 | 8 |
| α-helix | 61 | 1 | |
| β-strand | 62-63 | 2 | 9 |
| 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 | 9 |
| α-helix | 134-135 | 2 | |
| α-helix | 140-156 | 17 | |
| α-helix | 161-191 | 31 | |
| α-helix | 203-223 | 21 | |
| α-helix | 225-235 | 11 | |
| α-helix | 240-244 | 5 | |
| α-helix | 246-255 | 10 | |
| α-helix | 261-280 | 20 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-301 | 15 | |
| α-helix | 303-308 | 6 | |
| α-helix | 312-318 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MBP-MCL1 chimera protein,Induced myeloid leukemia cell differentiation protein Mcl-1 | A | protein | 518 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), Q07820 (AlphaFold model) |
>4WMU_1 MBP-MCL1 chimera protein,Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A) GKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTGSELYRQSLEIISRYLREQATGAADTAPMGASGATSRKALETLRRVGDGVQRN HETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQ ESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 19H | 6-chloro-3-[3-(4-chloro-3,5-dimethylphenoxy)propyl]-1H-indole-2-carboxylic acid | C20 H19 Cl2 N O3 | 1 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (FMT, NA, EDO) are not listed.
A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1. Clifton, M.C., Dranow, D.M., Leed, A. et al. PLoS One (2015) 10:e0125010-e0125010. DOI 10.1371/journal.pone.0125010 · 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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