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Literature summary extracted from

  • Doucet, N.; Jayasundera, T.; Simonovic, M.; Loria, J.
    The crystal structure of ribonuclease a in complex with thymidine-3'-monophosphate provides further insight into ligand binding (2010), Proteins, 78, 2459-2468.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.18 ribonuclease A in complex with thymidine 3'-monophosphate, hanging drop vapor diffusion method, 0.002 ml of 80 mg/ml protein in 20% ethanol and 20% acetic acid at pH 5.5, is mixed with 0.004 ml of 3'-TMP dissolved in a mother liquor solution of 20% ammonium sulfate and 2 M sodium chloride at pH 5.5, room temperature, 1 week, X-ray diffraction structure determination and analysis at 1.55 A resolution, molecular replacement, modelling Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.18 3'-CMP natural product inhibitor, NMR binding analysis, overview Bos taurus
4.6.1.18 3'-TMP a competitive inhibitor analogue of the 3'-CMP and 3'-UMP natural product inhibitors, the enzyme shows very high affinty and strong binding with 3'-TMP. Binding of 3'-TMP is very similar to other natural and nonnatural pyrimidine ligands, so single nucleotide affinity is independent of the presence or absence of a 2'-hydroxyl on the ribose moiety of pyrimidines Bos taurus
4.6.1.18 3'-UMP natural product inhibitor, NMR binding analysis, overview Bos taurus
4.6.1.18 additional information enzyme-inhibitor binding and interaction analysis, kinetics, overview Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus P61823
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 commercial preparation
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 Bos taurus
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4.6.1.18 pancreas
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 Bos taurus
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Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 pancreatic ribonuclease A
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 Bos taurus
4.6.1.18 RNase A
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 Bos taurus

General Information

EC Number General Information Comment Organism
4.6.1.18 additional information very subtle structural, chemical, and potentially motional variations contribute to ligand discrimination in the enzyme Bos taurus