1fpd | pdb_00001fpd

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

Template:STRUCTURE 1fpd

File:1fpd.png

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

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

Page seeded by OCA on Tue Feb 17 00:57:07 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

[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

1fpd | pdb_00001fpd

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

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools