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Results for property: Residues Involved in Catalysis of 3-5' Exo

Detailed Results for Property

Use this page to examine all the the polymerases and references referring to the property: Residues Involved in Catalysis of 3-5' Exo.

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Polymerase Kingdom Family Reference Result Context
KOD1 Archaeon B Catalyzing "hot" reactions: enzymes from hyperthermophilic Archaea. 141Asp-Ile-Glu143 (Exo I), 210Asn-Gly-Asp-Asn-Phe-Asp215 (Exo II), 311Try-Ser-Met-Glu-Asp315 (Exo III)
Klenow fragment Eubacterium A Cocrystal structure of an editing complex of Klenow fragment with DNA. D355, E357, D424, D501
Klenow fragment Eubacterium A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. D424, D355, E357, D501
Klenow fragment Eubacterium A Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. D355, E357, D424, D501
Klenow fragment Eubacterium A Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. D355, E357, D424, D501
Klenow fragment Eubacterium A Structure of DNA polymerase I Klenow fragment bound to duplex DNA. D355, E357, D424, D501
Klenow fragment Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Asp355, Glu357, Asp424, and Asp501
Bsu Pol X Eubacterium X Characterization of a Bacillus subtilis 64-kDa DNA polymerase X potentially involved in DNA repair. H339, H341, H437, H465, H528, E410, E496 and D526
Sso PolB-1 Archaeon B Insights into DNA replication: the crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus. Asp231, Glu233, Asp413

Version:20241007

Using Polbase tables:

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Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

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It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.