Literature summary for 3.6.1.23 extracted from

Leveles, I.; N�meth, V.; Szab�, J.E.; Harmat, V.; Ny�ri, K.; Bendes, �.�.; Papp-K�d�r, V.; Zagyva, I.; R�na, G.; Ozohanics, O.; V�key, K.; T�th, J., V�rtessy, B.G.
Structure and enzymatic mechanism of a moonlighting dUTPase (2013), Acta Crystallogr. Sect. D, 69, 2298-2308.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of dUTPase trimer, to 2.1 A resolution. The phage-specific insert folds into a small beta-pleated mini-domain reaching out from the dUTPase core surface. The insert mini-domains jointly coordinate a single Mg2+ ion per trimer at the entrance to the threefold inner channel. Residue Asp95, is the metal-ion-coordinating moiety potentially involved in correct positioning of the insert. The insert has no major role in dUTP binding or cleavage	Dubowvirus dv11

Crystallization (Comment)

Organism

structure of dUTPase trimer, to 2.1 A resolution. The phage-specific insert folds into a small beta-pleated mini-domain reaching out from the dUTPase core surface. The insert mini-domains jointly coordinate a single Mg2+ ion per trimer at the entrance to the threefold inner channel. Residue Asp95, is the metal-ion-coordinating moiety potentially involved in correct positioning of the insert. The insert has no major role in dUTP binding or cleavage

Dubowvirus dv11

Organism

Organism	UniProt	Comment	Textmining
Dubowvirus dv11	Q8SDV3	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)