1EMH
CRYSTAL STRUCTURE OF HUMAN URACIL-DNA GLYCOSYLASE BOUND TO UNCLEAVED SUBSTRATE-CONTAINING DNA
Summary for 1EMH
Entry DOI | 10.2210/pdb1emh/pdb |
Related | 1AKZ 1SSP 2SSP 4SKN |
Descriptor | DNA (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 Keywords | alpha/beta fold, uracil-dna glycosylase, protein/dna, hydrolase-dna complex, hydrolase/dna |
Biological source | Homo sapiens (human) |
Cellular location | Isoform 1: Mitochondrion. Isoform 2: Nucleus: P13051 |
Total number of polymer chains | 3 |
Total formula weight | 31311.98 |
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 citation | Parikh, 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: 10805771DOI: 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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