› 6mi3

X-ray diffraction
1.78Å resolution

Structure of NEMO(51-112) with N- and C-terminal coiled-coil adaptors.

Released:
DOI: 10.2210/pdb6mi3/pdb
PDB entry 6mi3 coloured by chain, front view.
PDB entry 6mi3 coloured by chain, side view.
PDB entry 6mi3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface.
Barczewski AH, Ragusa MJ, Mierke DF, Pellegrini M
OpenAccess logo Sci Rep 9 2950 (2019)
PMID: 30814588

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195372 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NF-kappa-B essential modulator Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 14.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6K9 (Residues: 38-47, 48-129; Coverage: 22%)
Gene names: FIP3, IKBKG, NEMO
Sequence domains: NF-kappa-B essential modulator NEMO

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P21
Unit cell:
a: 64.48Å b: 33.62Å c: 76.87Å
α: 90° β: 115.04° γ: 90°
R-values:
R R work R free
0.244 0.243 0.266
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Molecular insights into the pathophysiology of doxorubicin-induced cardiotoxicity: a graphical representation.
Sangweni et al. (2022)
2 more

4 mentions without citation

Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.
Hameedi et al. (2022)
3 more