2iz1
From Proteopedia
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|PDB= 2iz1 |SIZE=350|CAPTION= <scene name='initialview01'>2iz1</scene>, resolution 2.30Å | |PDB= 2iz1 |SIZE=350|CAPTION= <scene name='initialview01'>2iz1</scene>, resolution 2.30Å | ||
|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= | + | |LIGAND= <scene name='pdbligand=ATR:2'-MONOPHOSPHOADENOSINE-5'-DIPHOSPHATE'>ATR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=RES:4-PHOSPHO-D-ERYTHRONOHYDROXAMIC+ACID'>RES</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= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iz1 OCA], [http://www.ebi.ac.uk/pdbsum/2iz1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iz1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Iulek, J.]] | [[Category: Iulek, J.]] | ||
[[Category: Sundaramoorthy, R.]] | [[Category: Sundaramoorthy, R.]] | ||
| - | [[Category: ATR]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: P33]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: RES]] | ||
[[Category: 6-phosphogluconate dehydrogenase]] | [[Category: 6-phosphogluconate dehydrogenase]] | ||
[[Category: gluconate utilization]] | [[Category: gluconate utilization]] | ||
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[[Category: pentose shunt]] | [[Category: pentose shunt]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:40 2008'' |
Revision as of 00:50, 31 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Phosphogluconate dehydrogenase (decarboxylating), with EC number 1.1.1.44 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
6PDH COMPLEXED WITH PEX INHIBITOR SYNCHROTRON DATA
Overview
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 Structure
2IZ1 is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
Reference
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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