C-terminal bzip domain of human C/EBPBETA with 16BP methylated oligonucleotide containing consensus recognition sequence-C2 crystal form

Structure

x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, D, B
• GOL · Glycerol · additive · chains C, 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 · 683 Ų buried · 2 hydrogen bonds · protein-protein
• C–D · 617 Ų buried · 55 hydrogen bonds · nucleic-nucleic
• B–C · 386 Ų buried · 7 hydrogen bonds · protein-nucleic
• B–D · 383 Ų buried · 13 hydrogen bonds · protein-nucleic
• A–D · 381 Ų buried · 7 hydrogen bonds · protein-nucleic

Modifications

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

Compared structures

• 6MG1 · 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 A against A, TM-score 0.79

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 6MG1 · PDBe 6MG1 · UniProt P17676