A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1

A Comparative Study of Uracil-DNA Glycosylases from Human and Herpes Simplex Virus Type 1.

MDLTNGGVSPAATSAPLDWTTFRRVFLIDDAWRPLMEPELANPLTAHLLAEYNRRCQTEEVLPPREDVFSWTRYCTPDEV
RVVIIGQNPYHHPGQAHGLAFSVRANVPPPPSLRNVLAAVKNCYPEARMSGHGCLEKWARDGVLLLNTTLTVKRGAAASH
SRIGWDRFVGGVIRRLAARRPGLVFMLWGTHAQNAIRPDPRVHCVLKFSNPSPLSKVPFGTCQHFLVANRYLETRSISPI
DWSV

URACIL-DEOXYRIBONUCLEIC ACID GLYCOSYLASE

MOL_ID: 1; MOLECULE: URACIL-DEOXYRIBONUCLEIC ACID GLYCOSYLASE; CHAIN: NULL; EC: 3.2.2.3; OTHER_DETAILS: ENCODED BY THE UL2 ORF OF HERPES SIMPLEX VIRUS TYPE 1

MOL_ID: 1; MOLECULE: URACIL-DEOXYRIBONUCLEIC ACID GLYCOSYLASE; CHAIN: NULL; EC: 3.2.2.3; HETEROGEN: URACIL; OTHER_DETAILS: ENCODED BY THE UL2 ORF OF HERPES SIMPLEX VIRUS TYPE 1

NUCLEOTIDE MIMICRY IN THE CRYSTAL STRUCTURE OF THE URACIL-DNA GLYCOSYLASE - URACIL GLYCOSYLASE INHIBITOR PROTEIN COMPLEX

CUTS URACIL RESIDUES FROM THE DNA.

ENGINEERED RESIDUE IN CHAIN A, ASP 178 TO ASN ENGINEERED RESIDUE IN CHAIN A, HIS 300 TO ASN

oligosaccharide with reducing-end-to-reducing-end glycosidic bond

RESIDUES 1 - 16 IN THIS MOLECULE DO NOT APPEAR IN THE ELECTRON DENSITY AND ARE PRESUMED TO BE DISORDERED.

HYDROLASE, URACIL DNA GLYCOSYLASE, DNA REPAIR, DNA DAMAGE, GLYCOSIDASE