Solution structure of MCL-1. Determined by solution NMR. Released 23 Nov 2004.
Explore 1WSX in 3D Show helices and sheets RCSB PDB PDBe
1WSX contains 8 α-helices and 0 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 | 154-172 | 19 | |
| α-helix | 175-176 | 2 | |
| α-helix | 185-215 | 31 | |
| α-helix | 224-234 | 11 | |
| α-helix | 242-261 | 20 | |
| α-helix | 265-282 | 18 | |
| α-helix | 284-289 | 6 | |
| α-helix | 293-299 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| myeloid cell leukemia sequence 1 | A | protein | 162 | Mus musculus | P97287 (AlphaFold model) |
>1WSX_1 myeloid cell leukemia sequence 1 (chains A) GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE TAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQES FIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGG
Solution Structure of Prosurvival Mcl-1 and Characterization of Its Binding by Proapoptotic BH3-only Ligands. Day, C.L., Chen, L., Richardson, S.J. et al. J Biol Chem (2005) 280:4738-4744. DOI 10.1074/jbc.M411434200 · PubMed
Other PDB entries of the same protein (UniProt P97287 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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