5o0v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==crystal structure of E. coli GAP-DH by fortuitous crystallization as an impurity from a solution of human liver FBPase== | |
| - | + | <StructureSection load='5o0v' size='340' side='right' caption='[[5o0v]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5o0v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O0V FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o0v OCA], [http://pdbe.org/5o0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o0v RCSB], [http://www.ebi.ac.uk/pdbsum/5o0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o0v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/G3P1_ECO57 G3P1_ECO57]] Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.[UniProtKB:P0A9B2] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Benz, J]] | ||
| + | [[Category: Rudolph, M G]] | ||
[[Category: Ruf, A]] | [[Category: Ruf, A]] | ||
| - | [[Category: | + | [[Category: Fortuitous crystallization]] |
| - | [[Category: | + | [[Category: Immune system]] |
| + | [[Category: Impurity]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 10:04, 10 September 2017
crystal structure of E. coli GAP-DH by fortuitous crystallization as an impurity from a solution of human liver FBPase
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