2fmz
From Proteopedia
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===Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.=== | ===Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.=== | ||
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{{ABSTRACT_PUBMED_16686544}} | {{ABSTRACT_PUBMED_16686544}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2fmz]] is a 1 chain structure of [[Carbonic anhydrase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMZ OCA]. | |
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| + | ==See Also== | ||
| + | *[[Carbonic anhydrase|Carbonic anhydrase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016686544</ref><references group="xtra"/> |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Activator]] | [[Category: Activator]] | ||
[[Category: Carbonic anhydrase]] | [[Category: Carbonic anhydrase]] | ||
| - | [[Category: Crystal structure]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:38:28 2009'' | ||
Revision as of 04:04, 27 July 2012
Contents |
Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.
Template:ABSTRACT PUBMED 16686544
About this Structure
2fmz is a 1 chain structure of Carbonic anhydrase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Temperini C, Scozzafava A, Vullo D, Supuran CT. Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design. J Med Chem. 2006 May 18;49(10):3019-27. PMID:16686544 doi:10.1021/jm0603320
