Structure for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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! number | ! number | ||
! PDB code | ! PDB code | ||
! structural similarity (RMSD) (better if zero) | ! structural similarity (RMSD) (better if zero) | ||
! seuqence identity (%IDE) (better if 100%) | ! seuqence identity (%IDE) (better if 100%) | ||
! protein name | |||
! comments | ! comments | ||
|- | |- | ||
| 2 | | 2 | ||
| 1pw5 | | 1pw5 | ||
| 2.9 | | 2.9 | ||
| 25 | | 25 | ||
| STRUCTURAL GENOMICS, UNKNOWN FUNCTION, nagd protein, pu | |||
| Could be a hydrolase, not sure | | Could be a hydrolase, not sure | ||
|- | |- | ||
| 3 | | 3 | ||
| 2hx1 | | 2hx1 | ||
| 4.7 | | 4.7 | ||
| 23 | | 23 | ||
| HYDROLASE: predicted sugar phosphatases of the had superfamily | |||
| 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) | ||
|- | |- | ||
| 4 | | 4 | ||
|1o03 | |1o03 | ||
| 2.5 | | 2.5 | ||
| 24 | | 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) | | 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) | ||
|- | |- |
Revision as of 06:01, 8 May 2007
Structure similarity Table (results from dali search)
number | PDB code | structural similarity (RMSD) (better if zero) | seuqence identity (%IDE) (better if 100%) | protein name | comments |
---|---|---|---|---|---|
2 | 1pw5 | 2.9 | 25 | STRUCTURAL GENOMICS, UNKNOWN FUNCTION, nagd protein, pu | Could be a hydrolase, not sure |
3 | 2hx1 | 4.7 | 23 | HYDROLASE: predicted sugar phosphatases of the had superfamily | 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) |
22 | 2fpx | 3.3 | 20 | HYDROLASE: histidine biosynthesis bifunctional protein | HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. (Pubmed) |