3ZKE: LC8

Structure of LC8 in complex with Nek9 peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Mar 2013.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
HOMO SAPIENS
Chains
12
Atoms
4,726
Mol. weight
69 kDa
Released
20 Mar 2013

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

Secondary structure: helices and β-sheets

3ZKE contains 12 α-helices and 30 β-strands across 12 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.

Chains A and K: 2 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand6-1271
α-helix15-3117
α-helix35-5016
β-strand54-69161
β-strand73-7861
β-strand81-8771
Chains B, D, F, H, J and L: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand942-94871
Chains C, E, G and I: 2 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand6-1381
α-helix15-3117
α-helix35-5016
β-strand54-69161
β-strand72-7871
β-strand81-8771

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dynein light chain 1, cytoplasmicA, C, E, G, I, Kprotein89HOMO SAPIENSP63167 (AlphaFold model)
NEK9 proteinB, D, F, H, J, Lprotein11HOMO SAPIENSQ8TD19 (AlphaFold model)
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>3ZKE_1 DYNEIN LIGHT CHAIN 1, CYTOPLASMIC (chains A, C, E, G, I, K)
MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGR
NFGSYVTHETKHFIYFYLGQVAILLFKSG
Sequence of entity 2 (B, D, F, H, J, L), FASTA
>3ZKE_2 NEK9 PROTEIN (chains B, D, F, H, J, L)
VGMHSKGTQTA

Primary citation

Structural Analysis of the Regulation of the Dynll/Lc8 Binding to Nek9 by Phosphorylation. Gallego, P., Velazquez-Campoy, A., Regue, L. et al. J Biol Chem (2013) 288:12283. DOI 10.1074/JBC.M113.459149 · PubMed

Other PDB entries of the same protein (UniProt P63167 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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