4op4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form== | |
| - | + | <StructureSection load='4op4' size='340' side='right'caption='[[4op4]], [[Resolution|resolution]] 1.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4op4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t6m 3t6m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OP4 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]] 1.651Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4op4 OCA], [https://pdbe.org/4op4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4op4 RCSB], [https://www.ebi.ac.uk/pdbsum/4op4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4op4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DAPE_VIBCH DAPE_VIBCH] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] | ||
| + | [[Category: Anderson WF]] | ||
| + | [[Category: Jedrzejczak R]] | ||
| + | [[Category: Joachimiak A]] | ||
| + | [[Category: Makowska-Grzyska M]] | ||
| + | [[Category: Nocek B]] | ||
Current revision
Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form
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