1xid: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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-[[Image:1xid.gif|left|200px]]
+{{Seed}}
+[[Image:1xid.png|left|200px]]
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 {{STRUCTURE_1xid|  PDB=1xid  |  SCENE=  }}
-'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''
+===MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE===
-==Overview==
+<!--
-Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299449}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299449 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299449}}
 ==About this Structure==
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 [[Category: Carrell, H L.]]
 [[Category: Glusker, J P.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:04:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:40:08 2008''