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Literature summary for 4.6.1.18 extracted from

  • Holloway, D.E.; Chavali, G.B.; Leonidas, D.D.; Baker, M.D.; Acharya, K.R.
    Influence of naturally-occurring 5’-pyrophosphate-linked substituents on the binding of adenylic inhibitors to ribonuclease a: an X-ray crystallographic study (2009), Biopolymers, 91, 995-1008.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.18

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop/vapor-diffusion method, 20% PEG 4000, 0,02 M sodium citrat buffer, pH 5.5, 16°C, pancreatic ribonuclease A-5’-ATP complex, resolution 1.70 A, pancreatic ribonuclease A-P3-bis(5’-adenosyl) triphosphate complex, resolution 2.40 A, pancreatic ribonuclease A-NADPH complex, resolution 1.70 A, pancreatic ribonuclease A-NADP complex, resolution 1.70 A, pancreatic ribonuclease A-pyrophosphte ion complex, resolution 1.80 A, space group C121 Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ATP 5Â’-ATP binds with the adenine occupying the B2 subsite in the manner of an RNA substrate but with the gamma-phosphate at the P1 subsite, crystal structure of the complex with pancreatic ribonuclease A Bos taurus
NADP+ crystal structure of the complex with pancreatic ribonuclease A Bos taurus
NADPH crystal structure of the complex with pancreatic ribonuclease A Bos taurus
P1,P3-bis(5'-adenosyl) triphosphate crystal structure of the complex with pancreatic ribonuclease A Bos taurus
Pyrophosphate crystal structure of the complex with pancreatic ribonuclease A Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P61823
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-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bos taurus
-

Synonyms

Synonyms Comment Organism
pancreatic ribonuclease A
-
 Bos taurus
ribonuclease A
-
 Bos taurus
RNase A
-
 Bos taurus