Structure for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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| The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. (pubmed) | | The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. (pubmed) | ||
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| 4 | |||
|1o03 | |1o03 | ||
| 2.5 | | 2.5 |
Revision as of 05:51, 8 May 2007
Structure similarity Table (results from dali search)
number | PDB code | protein name | structural similarity (RMSD) (better if zero) | seuqence identity (%IDE) (better if 100%) | comments |
---|---|---|---|---|---|
2 | 1pw5 | STRUCTURAL GENOMICS, UNKNOWN FUNCTION nagd protein, pu | 2.9 | 25 | Could be a hydrolase, not sure |
3 | 2hx1 | HYDROLASE: predicted sugar phosphatases of the had superfamily | 4.7 | 23 | The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. (pubmed) |
4 | 1o03 | 2.5 | 24 | ISOMERASE: beta-phosphoglucomutase (in lactococcus lactis) | Phosphoglucomutases catalyze the interconversion of D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction central to energy metabolism in all cells and to the synthesis of cell wall polysaccharides in bacterial cells. Two classes of phosphoglucomutases (alpha-PGM and beta-PGM) are distinguished on the basis of their specificity for alpha- and beta-glucose-1-phosphate. beta-PGM is a member of the haloacid dehalogenase (HAD) superfamily, which includes the sarcoplasmic Ca(2+)-ATPase, phosphomannomutase, and phosphoserine phosphatase. beta-PGM is unusual among family members in that the common phosphoenzyme intermediate exists as a stable ground-state complex in this enzyme. Herein we report, for the first time, the three-dimensional structure of a beta-PGM and the first view of the true phosphoenzyme intermediate in the HAD superfamily. (Pubmed) |