EC Number   |
Reference |
|---|
   3.1.4.58 | structure in a product complex with 2'-AMP, to 2.0 A resolution. The extended histidine-containing motifs 43HxTxxF48 and 125HxTxxR130 are important for the reaction-. His43-Nepsilon makes a hydrogen bond with the ribose O3' leaving group, thereby implicating His43 as a general acid catalyst. His125-Nepsilon coordinates the O-1-phosphate oxygen of the AMP 2'-phosphate, pointing to His125 as a general base catalyst. Arg130 makes bidentate contact with the AMP 2'-phosphate, suggesting a role in transition-state stabilization |
743778 |
| 3.1.4.58 | structure of the catalytic domain by NMR studies |
743134 |
| 3.1.4.58 | structure of the catalytic fragment, at 1.8 A resolution. The molecule is comprised of two topologically equivalent three-stranded antiparallel beta-sheets that are related by a pseudo 2fold symmetry. Each beta-sheet contains an H-X-T-X motif, which is strictly conserved among members of the 2H phosphoesterase superfamily. The catalytic mechanism employs the nucleophilic water molecule activated by His310 |
743085 |
| 3.1.4.58 | structure to 1.6 A resolution. The enzyme is in an open conformation in the absence of substrate |
749516 |
