Crystal structure of Mcl-1 in complex with 138E12 peptide, Lys-covalent antagonist. Determined by X-ray diffraction at 1.95 Å resolution. Released 30 Dec 2020.
Explore 6VBX in 3D Show helices and sheets RCSB PDB PDBe
6VBX 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 | 174-191 | 18 | |
| α-helix | 204-212 | 9 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-223 | 6 | |
| α-helix | 225-235 | 11 | |
| α-helix | 244-254 | 11 | |
| α-helix | 261-280 | 20 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-308 | 22 | |
| α-helix | 311-318 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-11 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Induced myeloid leukemia cell differentiation protein Mcl-1 | A | protein | 156 | Homo sapiens | Q07820 (AlphaFold model) |
| Synthetic peptide | B | protein | 13 | synthetic construct | O43521 (AlphaFold model) |
>6VBX_1 Induced myeloid leukemia cell differentiation protein Mcl-1 (chains A) GSHMDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETA FQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCI EPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVED
>6VBX_2 Synthetic peptide (chains B) XIAEQLRRIGDRF
Design, Synthesis, and Structural Characterization of Lysine Covalent BH3 Peptides Targeting Mcl-1. Gambini, L., Udompholkul, P., Baggio, C. et al. J Med Chem (2021) 64:4903-4912. DOI 10.1021/acs.jmedchem.1c00005 · PubMed
Other PDB entries of the same protein (UniProt Q07820 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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