1szj
From Proteopedia
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|PDB= 1szj |SIZE=350|CAPTION= <scene name='initialview01'>1szj</scene>, resolution 2.0Å | |PDB= 1szj |SIZE=350|CAPTION= <scene name='initialview01'>1szj</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=ACT:Active+Site+Residues+CYS+149+And+HIS+176'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Active+Site+Residues+CYS+149+And+HIS+176'>ACT</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |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] | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1szj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1szj OCA], [http://www.ebi.ac.uk/pdbsum/1szj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1szj RCSB]</span> | ||
}} | }} | ||
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[[Category: Lin, Z.]] | [[Category: Lin, Z.]] | ||
[[Category: Song, S.]] | [[Category: Song, S.]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: SO4]] | ||
[[Category: allosterism]] | [[Category: allosterism]] | ||
[[Category: d-glyceraldehyde-3-phosphate-dehydrogenase]] | [[Category: d-glyceraldehyde-3-phosphate-dehydrogenase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:07 2008'' |
Revision as of 20:49, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| 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 | ||||||
STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION
Overview
When the active-site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase is irradiated with ultraviolet light in the presence of NAD+, a fluorescent NAD derivative that is covalently linked to the enzyme is obtained. A preliminary crystallographic study of this fluorescent derivative, as well as of the native and the carboxymethylated enzymes from Palinurus versicolor, showed that they are isomorphous and belong to space group C2 as reported for the native enzyme from Palinurus vulgaris. The three forms of the enzyme, although they have identical unit cell parameters, differ considerably in their diffraction patterns, indicating marked differences in conformation in spite of the fact that they differ chemically only in a restricted region around the active site.
About this Structure
1SZJ is a Single protein structure of sequence from Palinurus versicolor. Full crystallographic information is available from OCA.
Reference
Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative., Song SY, Gao YG, Zhou JM, Tsou CL, J Mol Biol. 1983 Dec 5;171(2):225-8. PMID:6655693
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