C-terminal bZIP domain of human C/EBPbeta with 16bp Methylated Oligonucleotide Containing Consensus Recognition Sequence-C2 Crystal Form. Determined by X-ray diffraction at 1.75 Å resolution. Released 12 Dec 2018.
Explore 6MG1 in 3D Show helices and sheets RCSB PDB PDBe
6MG1 contains 2 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 | 272-329 | 58 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 272-330 | 59 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CCAAT/enhancer-binding protein beta | A, B | protein | 78 | Homo sapiens | P17676 (AlphaFold model) |
| 16-bp methylated oligonucleotide | C, D | DNA | 16 | Homo sapiens |
>6MG1_1 CCAAT/enhancer-binding protein beta (chains A, B) HMKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELST LRNLFKQLPEPLLASSGH
>6MG1_2 16-bp methylated oligonucleotide (chains C, D) TATATTGCGCAATATA
Structural basis for effects of CpA modifications on C/EBP beta binding of DNA. Yang, J., Horton, J.R., Wang, D. et al. Nucleic Acids Res (2019) 47:1774-1785. DOI 10.1093/nar/gky1264 · PubMed
Other PDB entries of the same protein (UniProt P17676 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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