Solution structure of MCL-1 complexed with NOXAB. Determined by solution NMR. Released 20 Mar 2007.
Explore 2JM6 in 3D Show helices and sheets RCSB PDB PDBe
2JM6 contains 9 α-helices and 0 β-strands across 2 chains. 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 | 71-93 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 153-172 | 20 | |
| α-helix | 185-215 | 31 | |
| α-helix | 223-234 | 12 | |
| α-helix | 242-261 | 20 | |
| α-helix | 265-282 | 18 | |
| α-helix | 284-289 | 6 | |
| α-helix | 293-300 | 8 | |
| α-helix | 303-304 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Noxa | A | protein | 27 | Mus musculus | Q9JM54 (AlphaFold model) |
| Myeloid cell leukemia-1 protein Mcl-1 homolog | B | protein | 162 | Mus musculus | P97287 (AlphaFold model) |
>2JM6_1 Noxa (chains A) PADLKDECAQLRRIGDKVNLRQKLLNM
>2JM6_2 Myeloid cell leukemia-1 protein Mcl-1 homolog (chains B) GPLGSEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHE TAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQES FIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGG
Structural insights into the degradation of Mcl-1 induced by BH3 domains. Czabotar, P.E., Lee, E.F., van Delft, M.F. et al. Proc Natl Acad Sci U S A (2007) 104:6217-6222. DOI 10.1073/pnas.0701297104 · PubMed
Other PDB entries of the same protein (UniProt Q9JM54 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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