Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.97
Description:3',5'-nucleoside bisphosphate phosphatase.
Cath: 1.10.150.650; 3.20.20.140;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.97
BRENDA Enzyme Link: BRENDA 3.1.3.97
KEGG Enzyme Link: KEGG3.1.3.97
BioCyc Enzyme Link: BioCyc 3.1.3.97
ExPASy Enzyme Link: ExPASy3.1.3.97
EC2PDB Enzyme Link: EC2PDB 3.1.3.97
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.97
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.97
IntEnz Enzyme Link: IntEnz 3.1.3.97
MEDLINE Enzyme Link: MEDLINE 3.1.3.97
MSA:

3.1.3.97;

Phylogenetic Tree:

3.1.3.97;

Uniprot:
M-CSA:
RHEA:43532 a ribonucleoside 3',5'-bisphosphate + H2O = a ribonucleoside 5'-phosphate + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Discovery of a Previously Unrecognized Ribonuclease from Escherichia coli That Hydrolyzes 5'-Phosphorylated Fragments of RNA.Ghodge SV, Raushel FM2015 May 1225871919
Prospecting for unannotated enzymes: discovery of a 3',5'-nucleotide bisphosphate phosphatase within the amidohydrolase superfamily.Cummings JA, Vetting M, Ghodge SV, Xu C, Hillerich B, Seidel RD, Almo SC, Raushel FM2014 Jan 2824401123