CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.130 | P-30 Protein |
|
3.10.130.10 | Ribonuclease A-like domain |
Domain Context
CATH Clusters
| Superfamily | Ribonuclease A-like domain |
| Functional Family | Ribonuclease pancreatic |
Enzyme Information
| 4.6.1.18 |
Pancreatic ribonuclease.
based on mapping to UniProt P61823
(1) An (RNA) containing cytidine + H(2)O = an (RNA)-3'-cytidine- 3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA). (2) An (RNA) containing uridine + H(2)O = an (RNA)-3'-uridine- 3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA).
-!- Specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds in RNA. -!- The reaction takes place in two steps, with the 2',3'-cyclic phosphodiester intermediates released from the enzyme at the completion of the first step. -!- Hydrolysis of these cyclic compounds occurs at a much slower rate through a reversal of the first step, in which the -OH group of water substitutes for the 2'-OH group of the ribose used in the first step, and does not take place until essentially all the susceptible 3',5'-phosphodiester bonds have been cyclised. -!- The enzyme can act as an endo- or exo ribonuclease. -!- Formerly EC 2.7.7.16, EC 3.1.4.22 and EC 3.1.27.5.
|
UniProtKB Entries (1)
| P61823 |
RNAS1_BOVIN
Bos taurus
Ribonuclease pancreatic
|
PDB Structure
| PDB | 1D5D |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics.
Biochemistry
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