1QGP
NMR STRUCTURE OF THE Z-ALPHA DOMAIN OF ADAR1, 15 STRUCTURES
Summary for 1QGP
Entry DOI | 10.2210/pdb1qgp/pdb |
Descriptor | PROTEIN (DOUBLE STRANDED RNA ADENOSINE DEAMINASE) (1 entity in total) |
Functional Keywords | z-alpha-z-dna binding domain, rna-editing, z-dna recognition, adar1, helix- turn-helix, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P55265 |
Total number of polymer chains | 1 |
Total formula weight | 8609.83 |
Authors | Schade, M.,Turner, C.J.,Kuehne, R.,Schmieder, P.,Lowenhaupt, K.,Herbert, A.,Rich, A.,Oschkinat, H. (deposition date: 1999-05-03, release date: 1999-10-19, Last modification date: 2023-12-27) |
Primary citation | Schade, M.,Turner, C.J.,Kuhne, R.,Schmieder, P.,Lowenhaupt, K.,Herbert, A.,Rich, A.,Oschkinat, H. The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. Proc.Natl.Acad.Sci.USA, 96:12465-12470, 1999 Cited by PubMed: 10535945DOI: 10.1073/pnas.96.22.12465 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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