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. | | 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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Revision as of 05:40, 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 supeerfamily | 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) |
