Structure for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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! PDB code | ! PDB code | ||
! protein name | ! protein name | ||
! structural similarity (RMSD) | ! structural similarity (RMSD) (better if zero) | ||
! seuqence identity (%IDE) | ! seuqence identity (%IDE) (better if 100%) | ||
! comments | ! comments | ||
|- | |- | ||
| | | 2 | ||
| 1pw5 | | 1pw5 | ||
| STRUCTURAL GENOMICS, UNKNOWN FUNCTION nagd protein, pu | | STRUCTURAL GENOMICS, UNKNOWN FUNCTION nagd protein, pu | ||
Line 20: | Line 20: | ||
| Could be a hydrolase, not sure | | Could be a hydrolase, not sure | ||
|- | |- | ||
| 3 | |||
| 2hx1 | |||
| | |||
| | |||
| 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. | |||
|} | |} |
Revision as of 05:33, 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 | 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. |