1UTU: Novel protein EMSY truncate

Crystal structure of novel protein EMSY truncate. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Oct 2005.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,635
Mol. weight
24.47 kDa
Released
13 Oct 2005

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

Secondary structure: helices and β-sheets

1UTU contains 12 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix13-3826
α-helix43-5513
α-helix60-7213
α-helix74-8411
α-helix90-956
α-helix98-1014
Chain B: 6 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix13-3826
α-helix41-422
α-helix43-5513
α-helix60-7112
α-helix74-8411
α-helix90-956

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
EmsyA, Bprotein108HOMO SAPIENSQ7Z589 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1UTU_1 EMSY (chains A, B)
MPVVWPTLLDLSRDECKRILRKLELEAYAGVISALRAQGDLTKEKKDLLGELSKVLSIST
ERHRAEVRRAVNDERLTTIAHNMSGPNSSSEWSIEGRRLVPLMPRLVP

Primary citation

Binding of Emsy to Hp1Beta: Implications for Recruitment of Hp1Beta and Bs69. Ekblad, C.M., Chavali, G.B., Basu, B.P. et al. EMBO Rep (2005) 6:675. DOI 10.1038/SJ.EMBOR.7400415 · PubMed

Other PDB entries of the same protein (UniProt Q7Z589 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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