› 3brt

X-ray diffraction
2.25Å resolution

NEMO/IKK association domain structure

Released:
DOI: 10.2210/pdb3brt/pdb
PDB entry 3brt coloured by chain, front view.
PDB entry 3brt coloured by chain, side view.
PDB entry 3brt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site.
Rushe M, Silvian L, Bixler S, Chen LL, Cheung A, Bowes S, Cuervo H, Berkowitz S, Zheng T, Guckian K, Pellegrini M, Lugovskoy A
Structure 16 798-808 (2008)
PMID: 18462684

Function and Biology Details

Reactions catalysed: 
ATP + a protein = ADP + a phosphoprotein
ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein]
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-238620 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Inhibitor of nuclear factor kappa-B kinase subunit alpha; Inhibitor of nuclear factor kappa-B kinase subunit beta Chains: A, C
Molecule details ›
Chains: A, C
Length: 47 amino acids
Theoretical weight: 5.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14920 (Residues: 701-730; Coverage: 4%)
  • Canonical: O15111 (Residues: 732-745; Coverage: 2%)
Gene names: CHUK, IKBKB, IKKA, IKKB, TCF16
Sequence domains: I-kappa-kinase-beta NEMO binding domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
NF-kappa-B essential modulator Chains: B, D
Molecule details ›
Chains: B, D
Length: 68 amino acids
Theoretical weight: 8.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y6K9 (Residues: 44-111; Coverage: 16%)
Gene names: FIP3, IKBKG, NEMO
Sequence domains: NF-kappa-B essential modulator NEMO
Structure domains: L1 transposable element, trimerization domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 41.869Å b: 105.556Å c: 56.707Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.238 0.282
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

17 review citations

Molecular basis of NF-κB signaling.
Napetschnig et al. (2013)
16 more

22 mentions without citation

Structural studies of NF-κB signaling.
Zheng et al. (2011)
21 more