3PSE: Viral OTU domain protease

Structure of a viral OTU domain protease bound to interferon-stimulated gene 15 (ISG15). Determined by X-ray diffraction at 2.3 Å resolution. Released 19 Jan 2011.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Crimean-Congo hemorrhagic fever virus, Homo sapiens
Chains
2
Atoms
2,589
Mol. weight
36.83 kDa
Ligands
4LJ
Released
19 Jan 2011

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

Secondary structure: helices and β-sheets

3PSE contains 20 α-helices and 23 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: 9 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix1-55
β-strand10-1341
β-strand16-1941
β-strand2412
α-helix25-273
β-strand29-3241
α-helix40-4910
α-helix58-7215
α-helix73-753
α-helix79-824
α-helix86-938
β-strand10113
α-helix102-11110
β-strand116-12161
β-strand12612
β-strand127-13371
β-strand142-14761
β-strand151-15771
α-helix159-1613
Chain B: 11 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand5-954
β-strand15-1734
α-helix25-3612
α-helix40-423
β-strand43-4864
α-helix521
β-strand5314
α-helix54-552
α-helix60-623
β-strand70-7564
β-strand82-8765
β-strand93-9865
β-strand10316
α-helix104-11512
α-helix119-1213
β-strand122-12655
β-strand129-13025
α-helix131-1322
β-strand13616
α-helix137-1404
α-helix1461
β-strand147-15265
α-helix1531
β-strand15513

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA polymeraseAprotein171Crimean-Congo hemorrhagic fever virusQ6TQR6 (AlphaFold model)
Ubiquitin-like protein ISG15Bprotein156Homo sapiensP05161 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3PSE_1 RNA polymerase (chains A)
GPMDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSY
HYIKRLTESAARKYYQEEPEARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIII
WTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQFETDTREAL
Sequence of entity 2 (B), FASTA
>3PSE_2 Ubiquitin-like protein ISG15 (chains B)
MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPL
ASQGLGPGSTVLLVVDKSDEPLNILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDD
LFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRG

Ligands and cofactors

IDNameFormulaCopies
4LJ1.7.6 3-bromanylpropan-1-amineC3 H8 Br N1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural basis for the removal of ubiquitin and interferon-stimulated gene 15 by a viral ovarian tumor domain-containing protease. James, T.W., Frias-Staheli, N., Bacik, J.P. et al. Proc Natl Acad Sci U S A (2011) 108:2222-2227. DOI 10.1073/pnas.1013388108 · PubMed

Other PDB entries of the same protein (UniProt Q6TQR6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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