1UDG

THE STRUCTURAL BASIS OF SPECIFIC BASE EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE

Summary for 1UDG

Entry DOI	10.2210/pdb1udg/pdb
Descriptor	URACIL-DNA GLYCOSYLASE, SULFATE ION (3 entities in total)
Functional Keywords	hydrolase
Biological source	Herpes simplex virus (type 1 / strain 17)
Total number of polymer chains	1
Total formula weight	27558.57
Authors	Pearl, L.H.,Savva, R. (deposition date: 1995-06-23, release date: 1996-01-29, Last modification date: 2024-02-14)
Primary citation	Savva, R.,McAuley-Hecht, K.,Brown, T.,Pearl, L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature, 373:487-493, 1995 Cited by PubMed Abstract: The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision. PubMed: 7845459 DOI: 10.1038/373487a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation