IndraLab

Statements

sparser
"In the crystal structure of the Ser177-phosphorylated form of OTUD5 bound with ubiquitin ( xref ), the phosphate group has intramolecular interactions with other OTUD5 polar residues (including Arg272), and also has intermolecular interactions with the C-terminal tail of the bound ubiquitin, precisely orienting its C-terminus for catalysis."
33748114
sparser
"The crystal structure of the Ub-aldehyde complex with phosphorylated OTUD5 reveals a remarkable interaction between the phosphorylated Ser177 of OTUD5 and the guanidinium moiety of Arg74 of the bound ubiquitin showing that the phosphorylation is essential for the DUB activity [ xref ]."
32512887
sparser
"In the crystal structure of OTUD5 bound with ubiquitin ( xref ), Asp256, Arg274, and Asn293 are located on the surface of the protein, and form no direct interactions with ubiquitin ( xref )."
33748114