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1j0x

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|PDB= 1j0x |SIZE=350|CAPTION= <scene name='initialview01'>1j0x</scene>, resolution 2.4&Aring;
|PDB= 1j0x |SIZE=350|CAPTION= <scene name='initialview01'>1j0x</scene>, resolution 2.4&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|LIGAND= <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0x OCA], [http://www.ebi.ac.uk/pdbsum/1j0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j0x RCSB]</span>
}}
}}
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[[Category: Kaufmann, M.]]
[[Category: Kaufmann, M.]]
[[Category: Stark, W.]]
[[Category: Stark, W.]]
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[[Category: NAD]]
 
[[Category: apoptosis]]
[[Category: apoptosis]]
[[Category: dehydrogenase]]
[[Category: dehydrogenase]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:22 2008''

Revision as of 18:27, 30 March 2008


PDB ID 1j0x

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands: , ,
Activity: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)


Overview

The crystal structure of the tetrameric form of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isolated from rabbit muscle was solved at 2.4 A resolution after careful dynamic light-scattering experiments to find a suitable buffer for crystallization trials. The refined model has a crystallographic R factor of 20.3%. Here, the first detailed model of a mammalian GAPDH is presented. The cofactor NAD(+) (nicotinamide adenine dinucleotide) is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD(+) binding to this enzyme. The structure of rabbit-muscle GAPDH is of interest because it shares 91% sequence identity with the human enzyme; human GAPDH is a potential target for the development of anti-apoptotic drugs. In addition, differences in the cofactor-binding pocket compared with the homology-model structure of GAPDH from the malaria parasite Plasmodium falciparum could be exploited in order to develop novel selective and potential antimalaria drugs.

About this Structure

1J0X is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase., Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2218-27. Epub 2003, Nov 27. PMID:14646080

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