3lba
From Proteopedia
(Difference between revisions)
m (Protected "3lba" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:3lba.jpg|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3lba", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3lba| PDB=3lba | SCENE= }} | {{STRUCTURE_3lba| PDB=3lba | SCENE= }} | ||
| - | |||
===The Crystal Structure of smu.1229 from Streptococcus mutans UA159 bound to hypoxanthine=== | ===The Crystal Structure of smu.1229 from Streptococcus mutans UA159 bound to hypoxanthine=== | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/Q8DTU4_STRMU Q8DTU4_STRMU]] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477] | ||
==About this Structure== | ==About this Structure== | ||
| Line 20: | Line 13: | ||
[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: Wang, H F.]] | [[Category: Wang, H F.]] | ||
| + | [[Category: Glycosyltransferase]] | ||
| + | [[Category: Puna]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 20:29, 4 April 2013
The Crystal Structure of smu.1229 from Streptococcus mutans UA159 bound to hypoxanthine
Function
[Q8DTU4_STRMU] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477]
About this Structure
3lba is a 1 chain structure with sequence from Streptococcus mutans. Full crystallographic information is available from OCA.
