2iz0: Difference between revisions

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|PDB= 2iz0 |SIZE=350|CAPTION= <scene name='initialview01'>2iz0</scene>, resolution 2.60&Aring;
|PDB= 2iz0 |SIZE=350|CAPTION= <scene name='initialview01'>2iz0</scene>, resolution 2.60&Aring;
|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=RES:4-PHOSPHO-D-ERYTHRONOHYDROXAMIC+ACID'>RES</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=ATR:2'-MONOPHOSPHOADENOSINE-5'-DIPHOSPHATE'>ATR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=RES:4-PHOSPHO-D-ERYTHRONOHYDROXAMIC+ACID'>RES</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=ATR:2&#39;-MONOPHOSPHOADENOSINE-5&#39;-DIPHOSPHATE'>ATR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphogluconate_dehydrogenase_(decarboxylating) Phosphogluconate dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.44 1.1.1.44]  
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphogluconate_dehydrogenase_(decarboxylating) Phosphogluconate dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.44 1.1.1.44]  
|GENE=  
|GENE=  
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[[Category: pentose shunt]]
[[Category: pentose shunt]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:23:23 2008''

Revision as of 16:23, 23 March 2008

File:2iz0.gif


PDB ID 2iz0

Drag the structure with the mouse to rotate
, resolution 2.60Å
Sites:
Ligands: , , , , , , and
Activity: Phosphogluconate dehydrogenase (decarboxylating), with EC number 1.1.1.44
Coordinates: save as pdb, mmCIF, xml



PEX INHIBITOR-HOME DATA


OverviewOverview

Crystal structures of recombinant Lactococcus lactis 6-phosphogluconate dehydrogenase (LlPDH) in complex with substrate, cofactor, product and inhibitors have been determined. LlPDH shares significant sequence identity with the enzymes from sheep liver and the protozoan parasite Trypanosoma brucei for which structures have been reported. Comparisons indicate that the key residues in the active site are highly conserved, as are the interactions with the cofactor and the product ribulose 5-phosphate. However, there are differences in the conformation of the substrate 6-phosphogluconate which may reflect distinct states relevant to catalysis. Analysis of the complex formed with the potent inhibitor 4-phospho-d-erythronohydroxamic acid, suggests that this molecule does indeed mimic the high-energy intermediate state that it was designed to. The analysis also identified, as a contaminant by-product of the inhibitor synthesis, 4-phospho-d-erythronamide, which binds in similar fashion. LlPDH can now serve as a model system for structure-based inhibitor design targeting the enzyme from Trypanosoma species.

About this StructureAbout this Structure

2IZ0 is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates., Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN, FEBS J. 2007 Jan;274(1):275-86. PMID:17222187

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