2bif: Difference between revisions
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[[Image:2bif.png|left|200px]] | [[Image:2bif.png|left|200px]] | ||
{{STRUCTURE_2bif| PDB=2bif | SCENE= }} | {{STRUCTURE_2bif| PDB=2bif | SCENE= }} | ||
===6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE=== | ===6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE=== | ||
{{ABSTRACT_PUBMED_9890980}} | {{ABSTRACT_PUBMED_9890980}} | ||
==About this Structure== | ==About this Structure== | ||
[[2bif]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIF OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:009890980</ref><references group="xtra"/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Hasemann, C A.]] | [[Category: Hasemann, C A.]] | ||
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[[Category: Bifunctional enzyme]] | [[Category: Bifunctional enzyme]] | ||
[[Category: Glycolysis]] | [[Category: Glycolysis]] | ||
[[Category: Hydrolase]] | |||
[[Category: Kinase]] | [[Category: Kinase]] | ||
[[Category: Phosphatase]] | [[Category: Phosphatase]] | ||
[[Category: Transferase]] | |||
Revision as of 14:30, 6 January 2013
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE
Template:ABSTRACT PUBMED 9890980
About this StructureAbout this Structure
2bif is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Yuen MH, Mizuguchi H, Lee YH, Cook PF, Uyeda K, Hasemann CA. Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities. J Biol Chem. 1999 Jan 22;274(4):2176-84. PMID:9890980