2KXR: ZO1 ZU5 domain MC/AA mutation

ZO1 ZU5 domain MC/AA mutation. Determined by solution NMR. Released 30 Mar 2011.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
892
Mol. weight
12.69 kDa
Released
30 Mar 2011

Explore 2KXR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KXR contains 2 α-helices and 8 β-strands across 1 chain. 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: 2 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand3-1081
β-strand15-1842
β-strand25-2842
β-strand39-4681
α-helix52-543
β-strand6311
β-strand68-6921
β-strand76-85102
α-helix102-1043
β-strand111-11772

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tight junction protein ZO-1Aprotein118Homo sapiensQ07157 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KXR_1 Tight junction protein ZO-1 (chains A)
TVVATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGVEQEIYFKVCRDNSILPPLDKEKG
ETLLSPLVAAGPHGLKFLKPVELRLPHCDPKTWQNKCLPGDPNYLVGANCVSVLIDHF

Primary citation

Cdc42-dependent formation of the ZO-1/MRCKb complex at the leading edge controls cell migration. Huo, L., Wen, W., Wang, R. et al. EMBO J (2011) 30:665-678. DOI 10.1038/emboj.2010.353 · PubMed

Other PDB entries of the same protein (UniProt Q07157 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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