3F89: NEMO CoZi domain

NEMO CoZi domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 24 Mar 2009.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,453
Mol. weight: 21.55 kDa
Released: 24 Mar 2009

Explore 3F89 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3F89 contains 6 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	260-278	19
α-helix	280-287	8
α-helix	290-321	32
α-helix	323-328	6
α-helix	330-333	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	260-334	75

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NF-kappa-B essential modulator	A, B	protein	92	Mus musculus	O88522 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3F89_1 NF-kappa-B essential modulator (chains A, B)
GSGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHNIVMETVPVLKAQADIYKADFQA
ERHAREKLVEKKEYLQEQLEQLQREFNKLKVG

Primary citation

Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Rahighi, S., Ikeda, F., Kawasaki, M. et al. Cell (2009) 136:1098-1109. DOI 10.1016/j.cell.2009.03.007 · PubMed

Other PDB entries of the same protein (UniProt O88522 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4OWF 2.0 Å, Crystal structure of the NEMO CoZi in complex with HOIP NZF1 domain
3JSV 2.7 Å, Crystal structure of mouse NEMO CoZi in complex with Lys63-linked di-ubiquitin
2V4H 2.9 Å, NEMO CC2-LZ domain - 1D5 DARPin complex
2ZVO 2.9 Å, NEMO CoZi domain in complex with diubiquitin in C2 space group
2ZVN 3.0 Å, NEMO CoZi domain incomplex with diubiquitin in P212121 space group

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