1eug Summary

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CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED

The structure was published by Xiao, G., Tordova, M., Jagadeesh, J., Drohat, A.C., Stivers, J.T., and Gilliland, G.L., in 1999 in a paper entitled "Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PROTEIN (GLYCOSYLASE). This molecule has the UniProt identifier P12295 (UNG_ECOLI)search. The sample contained 229 residues which is 100% of the natural sequence. Out of 229 residues 225 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PROTEIN (GLYCOSYLASE) P12295 (1-229) (UNG_ECOLI)search Escherichia coli K-12search 100% 229 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12295 (1 - 229) PROTEIN (GLYCOSYLASE) Escherichia coli B

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P12295) Uracil-DNA glycosylasesearch Uracil-DNA Glycosylase, subunit Esearch PF03167: Uracil DNA glycosylase superfamilysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P12295) uracil DNA N-glycosylase activitysearch hydrolase activity, hydrolyzing N-glycosyl compoundssearch protein bindingsearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch base-excision repairsearch DNA repairsearch cellular response to DNA damage stimulussearch metabolic processsearch cytoplasmsearch

Chain InterPro annotation
A Uracil-DNA glycosylasesearch Uracil-DNA glycosylase-likesearch Uracil-DNA glycosylase, active sitesearch