1tg3
From Proteopedia
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===Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II=== | ===Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II=== | ||
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- | ==Disease== | ||
- | Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611492 611492]] | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[1tg3]] 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=1TG3 OCA]. | |
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+ | ==See Also== | ||
+ | *[[Carbonic anhydrase|Carbonic anhydrase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015667203</ref><references group="xtra"/> |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Tu, C K.]] | [[Category: Tu, C K.]] | ||
[[Category: Yoshioka, C.]] | [[Category: Yoshioka, C.]] | ||
+ | [[Category: Lyase]] | ||
[[Category: Proton shuttle carbonic anhydrase metalloenzyme]] | [[Category: Proton shuttle carbonic anhydrase metalloenzyme]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:54:28 2009'' |
Revision as of 14:01, 25 July 2012
Contents |
Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
Template:ABSTRACT PUBMED 15667203
About this Structure
1tg3 is a 1 chain structure of Carbonic anhydrase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry. 2005 Feb 1;44(4):1097-105. PMID:15667203 doi:10.1021/bi0480279