Mcl-1 in complex with Bim BH3 mutant I2dY. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Feb 2010.
Explore 3KJ0 in 3D Show helices and sheets RCSB PDB PDBe
3KJ0 contains 11 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 | 173-191 | 19 | |
| α-helix | 203-223 | 21 | |
| α-helix | 225-235 | 11 | |
| α-helix | 240-253 | 14 | |
| α-helix | 261-280 | 20 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-295 | 9 | |
| α-helix | 296-300 | 5 | |
| α-helix | 301-308 | 8 | |
| α-helix | 311-318 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-21 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Induced myeloid leukemia cell differentiation protein Mcl-1 | A | protein | 158 | Homo sapiens | Q07820 (AlphaFold model) |
| Bcl-2-like protein 11 | B | protein | 27 | Homo sapiens | O43521 (AlphaFold model) |
>3KJ0_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A) GSDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQ GMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEP LAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGG
>3KJ0_2 Bcl-2-like protein 11 (chains B) GSGGRPEIWYAQELRRIGDEFNAYYAR
Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. Fire, E., Gulla, S.V., Grant, R.A. et al. Protein Sci (2010) 19:507-519. DOI 10.1002/pro.329 · PubMed
Other PDB entries of the same protein (UniProt Q07820 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3KJ0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.