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: 10535945 DOI: 10.1073/pnas.96.22.12465 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation