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1EMH

CRYSTAL STRUCTURE OF HUMAN URACIL-DNA GLYCOSYLASE BOUND TO UNCLEAVED SUBSTRATE-CONTAINING DNA

Summary for 1EMH
Entry DOI10.2210/pdb1emh/pdb
Related1AKZ 1SSP 2SSP 4SKN
DescriptorDNA (5'-D(*TP*GP*TP*(P2U)P*AP*TP*CP*TP*T)-3'), DNA (5'-D(*AP*AP*AP*GP*AP*TP*AP*AP*CP*A)-3'), URACIL-DNA GLYCOSYLASE, ... (4 entities in total)
Functional Keywordsalpha/beta fold, uracil-dna glycosylase, protein/dna, hydrolase-dna complex, hydrolase/dna
Biological sourceHomo sapiens (human)
Cellular locationIsoform 1: Mitochondrion. Isoform 2: Nucleus: P13051
Total number of polymer chains3
Total formula weight31311.98
Authors
Parikh, S.S.,Slupphaug, G.,Krokan, H.E.,Blackburn, G.M.,Tainer, J.A. (deposition date: 2000-03-16, release date: 2000-05-16, Last modification date: 2024-02-07)
Primary citationParikh, S.S.,Walcher, G.,Jones, G.D.,Slupphaug, G.,Krokan, H.E.,Blackburn, G.M.,Tainer, J.A.
Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects.
Proc.Natl.Acad.Sci.USA, 97:5083-5088, 2000
Cited by
PubMed: 10805771
DOI: 10.1073/pnas.97.10.5083
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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