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Crystal structure of ribonuclease T1 complexed with adenosine 2'-monophosphate at 1.8-A resolution.
Ding J, Koellner G, Grunert HP, Saenger W. Ding J, et al. Among authors: saenger w. J Biol Chem. 1991 Aug 15;266(23):15128-34. doi: 10.2210/pdb6rnt/pdb. J Biol Chem. 1991. PMID: 1651320 Free article.
The phosphate group of 2'-AMP is tightly hydrogen-bonded to the side chains of the active site residues Tyr38, His40, Glu58, Arg77, and His92, comparable with vanadate binding in the respective complex (Kostrewa, D., Choe, H.-W., Heinemann, U., and Saenger, W …
The phosphate group of 2'-AMP is tightly hydrogen-bonded to the side chains of the active site residues Tyr38, His40, Glu58, Arg77, and His9 …
Studies on RNase T1 mutants affecting enzyme catalysis.
Grunert HP, Zouni A, Beineke M, Quaas R, Georgalis Y, Saenger W, Hahn U. Grunert HP, et al. Among authors: saenger w. Eur J Biochem. 1991 Apr 10;197(1):203-7. doi: 10.1111/j.1432-1033.1991.tb15900.x. Eur J Biochem. 1991. PMID: 1901790 Free article.
335 results