C-terminal bzip domain of human C/EBPBETA with 16BP methylated oligonucleotide containing consensus recognition sequence-C2221 crystal form

Structure

x-ray diffraction · 3 distinct chains · 88% helix, 0% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · 2 copies · chains A, C, B, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–B · 976 Ų buried · 5 hydrogen bonds · protein-protein
• C–D · 722 Ų buried · 54 hydrogen bonds · nucleic-nucleic
• A–C · 399 Ų buried · 9 hydrogen bonds · protein-nucleic
• B–C · 374 Ų buried · 6 hydrogen bonds · protein-nucleic
• A–D · 354 Ų buried · 5 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 4 modified (nucleotide modification).

Compared structures

• 6MG2 · C-terminal bZIP domain of human C/EBPbeta with 16bp Methylated Oligonucleotide Containing… · the same entry in another collection · chain A against A, TM-score 1.00
• P17676 · AlphaFold monomer V2.0 prediction for CCAAT/ENHANCER-binding protein beta (P17676) · a predicted model of the same protein · chain B against A, TM-score 0.87

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P17676
• Elsewhere: RCSB PDB 6MG2 · PDBe 6MG2 · UniProt P17676