Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.6.1.15: nucleoside-triphosphate phosphatase

This is an abbreviated version!
For detailed information about nucleoside-triphosphate phosphatase, go to the full flat file.

Word Map on EC 3.6.1.15

Reaction

a nucleoside triphosphate
+
H2O
=
a nucleoside diphosphate
 +
phosphate

Synonyms

AAA-type nucleoside triphosphatase phosphohydrolase, ankyrin repeat-rich membrane spanning protein, cell division control protein Cdc48, DEAH-box Prp22 protein, DEAH-box splicing factor Prp22, DExH-Box NTPase, DR_0079, germ-cell-specific leucine-rich repeat protein, GP086L protein, HCR-NTPase, HrpB, HrpB NTPase, human cancer-related nucleoside triphosphatase, KAP NTPase, Kidins220, kinase D interacting substance of 220 kDa, LDBPK_100150, LdNTPDase2, LINF_150005200, LiNTPDase1, LMXM_10_0170, LMXM_15_0030, LmxNTPDase1, LmxNTPDase2, M86L protein, MC100R, Mg2+-dependent NTPase, More, Msm0858, NALP14, non-specific nucleoside triphosphatase, nonstructural protein 13, NPH I, NS3, NS3 protein, NS3FL, nsp13, NTP1, NTP3, NTPase, NTPase 1, NTPase 2, NTPase-I, NTPase-II, NTPase/helicase, NTPDase, NTPDase 1, NTPDase1, NTPDase2, nucleic acid-independent nucleoside triphosphatase, nucleoside 5-triphosphatase, nucleoside triphosphatase, nucleoside triphosphatase (NTPase)/helicase, nucleoside triphosphate diphospho-hydrolase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate diphosphohydrolase 1, nucleoside triphosphate hydrolase, nucleoside triphosphate hydrolases I, nucleoside triphosphate hydrolases II, nucleoside triphosphate phosphohydrolase, nucleoside triphosphate phosphohydrolase I, nucleoside-5-triphosphate phosphohydrolase, nucleoside-triphosphatase 1, nucleoside-triphosphatase 2, nucleotide 5'-triphosphatase, P-loop NTPase, phosphatase, nucleoside tri-, PilB, PilT, PilU, polypeptide p41, protein NS3, PVA coat protein, PVA CP, PVx coat protein, PVX CP, Rad55B, RNA-dependent nucleoside triphosphatase, SHVp41, Sso0909, T4P motor protein, type IV pilus motor protein, YtkD

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.15 nucleoside-triphosphate phosphatase

Crystallization

Crystallization on EC 3.6.1.15 - nucleoside-triphosphate phosphatase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determined in the metal-free form at 1.9 A resolution, data collection and structure refinement statistics, molscript ribbon representation of the crystal structure
purified recombinant selenomethionine-derivatized full-length enzyme, X-ray diffraction structrue determination and analysis. The final model of HrpBFL contains residues 1-805 without gaps and three additional residues (Ala-Met-Ala) at the N terminus that remained after tag cleavage. The overall structure of HrpBFL resembles a mushroom with a globular head module (residues 1-566) and an extended stalk (residues 567-805)
purified recombinant wild-type enzyme and SeMet-labeled enzyme, hanging drop vapor diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, and 10 mM DTT, with an equal volume of reservoir solution containing 0.3 M ammonium tartrate dibasic and 25% PEG 3350, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.5 and 3.2 A resolution, respectively
sitting drop vapor diffusion method, using 8-10% (w/v) PEG 3350, 0.1 M Tris-HCl pH 7.4, 50 mM diammonium phosphate and 2%(v/v) glycerol, at 20°C
sitting drop vapor diffusion method, using 10-12% (w/v) PEG 3350, 0.1 M Tris-HCl pH 7.4, 2% (v/v) glycerol, at 20°C