1fpd: Difference between revisions

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==About this Structure==
==About this Structure==
1FPD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPD OCA].  
1FPD is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPD OCA].  


==Reference==
==Reference==
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography., Villeret V, Huang S, Zhang Y, Lipscomb WN, Biochemistry. 1995 Apr 4;34(13):4307-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7703244 7703244]
<ref group="xtra">PMID:7703244</ref><references group="xtra"/>
[[Category: Fructose-bisphosphatase]]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Huang, S.]]
[[Category: Huang, S.]]
Line 32: Line 31:
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]


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Revision as of 22:57, 16 February 2009

File:1fpd.png

Template:STRUCTURE 1fpd

STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY

Template:ABSTRACT PUBMED 7703244

About this Structure

1FPD is a 2 chains structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

  1. Villeret V, Huang S, Zhang Y, Lipscomb WN. Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Biochemistry. 1995 Apr 4;34(13):4307-15. PMID:7703244

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