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1xya
From Proteopedia
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{{STRUCTURE_1xya| PDB=1xya | SCENE= }} | {{STRUCTURE_1xya| PDB=1xya | SCENE= }} | ||
===X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS=== | ===X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1xya]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_olivochromogenes Streptomyces olivochromogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3xia 3xia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYA OCA]. | |
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| + | ==See Also== | ||
| + | *[[D-xylose isomerase|D-xylose isomerase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008180169</ref><references group="xtra"/> |
[[Category: Streptomyces olivochromogenes]] | [[Category: Streptomyces olivochromogenes]] | ||
[[Category: Xylose isomerase]] | [[Category: Xylose isomerase]] | ||
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[[Category: Petsko, G A.]] | [[Category: Petsko, G A.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
| - | + | [[Category: Isomerase]] | |
| - | + | [[Category: Oxidoreductase]] | |
Revision as of 11:45, 5 January 2013
Contents |
X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Template:ABSTRACT PUBMED 8180169
About this Structure
1xya is a 2 chain structure with sequence from Streptomyces olivochromogenes. This structure supersedes the now removed PDB entry 3xia. Full crystallographic information is available from OCA.
See Also
Reference
- Lavie A, Allen KN, Petsko GA, Ringe D. X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry. 1994 May 10;33(18):5469-80. PMID:8180169
