Arginine kinase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 13: Line 13:
== Structural highlights ==
== Structural highlights ==
-
The <scene name='71/715906/Cv/4'>active site</scene> of AK is located between its N-terminal helical region and the larger C-terminal region. <ref>PMID:9671698</ref> Water molecules are shown as red spheres.
+
The <scene name='71/715906/Cv/3'>active site</scene> of AK is located between its N-terminal helical region and the larger C-terminal region. <ref>PMID:9671698</ref> Water molecules are shown as red spheres. <scene name='71/715906/Cv/4'>Mg+2 coordination site</scene>.
</StructureSection>
</StructureSection>

Revision as of 11:08, 6 January 2019

Arginine kinase complex with D-arginine (magenta), ADP (crimson), NO3- and Mg+2 ions and (PDB code 1bg0)

Drag the structure with the mouse to rotate

3D structures of arginine kinase

Updated on 06-January-2019

References

  1. Wang Z, Qiao Z, Ye S, Zhang R. Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains. Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):779-89. doi:, 10.1107/S1399004715001169. Epub 2015 Mar 26. PMID:25849389 doi:http://dx.doi.org/10.1107/S1399004715001169
  2. Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS. Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8449-54. PMID:9671698

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools