5loa
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+== | |
| - | + | <StructureSection load='5loa' size='340' side='right'caption='[[5loa]], [[Resolution|resolution]] 1.84Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5loa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | [[Category: Dunstan | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5loa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loa OCA], [https://pdbe.org/5loa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5loa RCSB], [https://www.ebi.ac.uk/pdbsum/5loa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5loa ProSAT]</span></td></tr> |
| - | [[Category: Gahloth | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DAPDH_CORGL DAPDH_CORGL] Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L-2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L-methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L-tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D-alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+).<ref>PMID:8865347</ref> <ref>PMID:8865347</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Corynebacterium glutamicum ATCC 13032]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dunstan MS]] | ||
| + | [[Category: Gahloth D]] | ||
Current revision
Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+
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