2kzr

Solution NMR

Solution NMR Structure of Ubiquitin thioesterase OTU1 (EC 3.1.2.-) from Mus musculus, Northeast Structural Genomics Consortium Target MmT2A

Released:
Source organism: Mus musculus
Entry authors: Chitayat S, Gutmanas A, Lemak A, Yee A, Bezsonova I, Wu B, Doherty RS, Semesi A, Montelione GT, Arrowsmith CH, Dhe-Paganon S, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-183946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin thioesterase OTU1 Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.36 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8CB27 (Residues: 42-127; Coverage: 25%)
Gene name: Yod1
Sequence domains: OTU1, UBXL domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)