1OTR: CUE-Ubiquitin Complex

Solution Structure of a CUE-Ubiquitin Complex. Determined by solution NMR. Released 24 Jun 2003.

Method: Solution NMR
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 990
Mol. weight: 14.14 kDa
Released: 24 Jun 2003

Explore 1OTR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OTR contains 6 α-helices and 5 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	9-19	11
α-helix	25-34	10
α-helix	40-49	10

Chain B: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	1
β-strand	12-16	5	1
α-helix	23-34	12
β-strand	41-45	5	1
β-strand	48-49	2	1
α-helix	50-51	2
α-helix	56-59	4
β-strand	66-71	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
protein Cue2	A	protein	49	Saccharomyces cerevisiae	P36075 (AlphaFold model)
Ubiquitin	B	protein	76	Saccharomyces cerevisiae	P0CG63 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1OTR_1 protein Cue2 (chains A)
NDDHESKLSILMDMFPAISKSKLQVHLLENNNDLDLTIGLLLKENDDKS

Sequence of entity 2 (B), FASTA

>1OTR_2 Ubiquitin (chains B)
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Solution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding. Kang, R.S., Daniels, C.M., Francis, S.A. et al. Cell (2003) 113:621-630. DOI 10.1016/S0092-8674(03)00362-3 · PubMed

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