5EP6: NAP1

The crystal structure of NAP1 in complex with TBK1. Determined by X-ray diffraction at 1.45 Å resolution. Released 28 Sept 2016.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Homo sapiens
Chains
4
Atoms
1,599
Mol. weight
24.37 kDa
Released
28 Sept 2016

Explore 5EP6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EP6 contains 4 α-helices and 5 β-strands across 4 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: 1 helix, 2 β-strands

ElementResiduesLengthSheet
α-helix216-24631
β-strand24711
β-strand248-24922
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix680-71435
β-strand715-71732
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix217-24630
Chain D: 1 helix, 2 β-strands
ElementResiduesLengthSheet
α-helix680-71435
β-strand715-71732
β-strand72311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
5-azacytidine-induced protein 2A, Cprotein47Homo sapiensQ9H6S1 (AlphaFold model)
Serine/threonine-protein kinase TBK1B, Dprotein58Homo sapiensQ9UHD2 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>5EP6_1 5-azacytidine-induced protein 2 (chains A, C)
SSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSTAIKKENLYFQ
Sequence of entity 2 (B, D), FASTA
>5EP6_2 Serine/threonine-protein kinase TBK1 (chains B, D)
SGSGSYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL

Primary citation

Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins. Li, F., Xie, X., Wang, Y. et al. Nat Commun (2016) 7:12708-12708. DOI 10.1038/ncomms12708 · PubMed

Other PDB entries of the same protein (UniProt Q9H6S1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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