6MG2: CCAAT/enhancer-binding protein beta

C-terminal bZIP domain of human C/EBPbeta with 16bp Methylated Oligonucleotide Containing Consensus Recognition Sequence-C2221 Crystal Form. Determined by X-ray diffraction at 1.93 Å resolution. Released 12 Dec 2018.

Method
X-ray diffraction
Resolution
1.93 Å
Organism
Homo sapiens
Chains
4
Atoms
2,071
Mol. weight
28.62 kDa
Released
12 Dec 2018

Explore 6MG2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MG2 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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix272-32857
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix272-33261

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CCAAT/enhancer-binding protein betaA, Bprotein78Homo sapiensP17676 (AlphaFold model)
16-bp methylated oligonucleotideC, DDNA16Homo sapiens
Sequence of entity 1 (A, B), FASTA
>6MG2_1 CCAAT/enhancer-binding protein beta (chains A, B)
HMKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELST
LRNLFKQLPEPLLASSGH
Sequence of entity 2 (C, D), FASTA
>6MG2_2 16-bp methylated oligonucleotide (chains C, D)
TATATTGCGCAATATA

Primary citation

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:

Browse structure collections

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