1xic

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{{STRUCTURE_1xic| PDB=1xic | SCENE= }}
{{STRUCTURE_1xic| PDB=1xic | SCENE= }}
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'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''
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===MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15299449 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299449}}
==About this Structure==
==About this Structure==
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[[Category: Carrell, H L.]]
[[Category: Carrell, H L.]]
[[Category: Glusker, J P.]]
[[Category: Glusker, J P.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:34:38 2008''

Revision as of 12:34, 28 July 2008

Image:1xic.png

Template:STRUCTURE 1xic

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

Template:ABSTRACT PUBMED 15299449

About this Structure

1XIC is a Single protein structure of sequence from Streptomyces rubiginosus. Full crystallographic information is available from OCA.

Reference

Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:15299449

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