6mfi
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6mfi is ON HOLD Authors: Selleck, C., Guddat, L., Schenk, G., Monteiro Pedroso, M. Description: MIM-2 Metallo-Beta-Lactamase [[Category: Unreleased...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==MIM-2 Metallo-Beta-Lactamase== | |
| + | <StructureSection load='6mfi' size='340' side='right'caption='[[6mfi]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mfi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simiduia_agarivorans_SA1_=_DSM_21679 Simiduia agarivorans SA1 = DSM 21679]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFI 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]] 1.839Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6mfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfi OCA], [https://pdbe.org/6mfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfi RCSB], [https://www.ebi.ac.uk/pdbsum/6mfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K4KM71_SIMAS K4KM71_SIMAS] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metallohydrolases are a vast family of enzymes that play crucial roles in numerous metabolic pathways. Several members have emerged as targets for chemotherapeutics. Knowledge about their reaction mechanisms and associated transition states greatly aids the design of potent and highly specific drug leads. By using a high-resolution crystal structure, we have probed the trajectory of the reaction catalyzed by purple acid phosphatase, an enzyme essential for the integrity of bone structure. In particular, the transition state is visualized, thus providing detailed structural information that may be exploited in the design of specific inhibitors for the development of new anti-osteoporotic chemotherapeutics. | ||
| - | + | Visualization of the Reaction Trajectory and Transition State in a Hydrolytic Reaction Catalyzed by a Metalloenzyme.,Selleck C, Clayton D, Gahan LR, Mitic N, McGeary RP, Pedroso MM, Guddat LW, Schenk G Chemistry. 2017 Apr 6;23(20):4778-4781. doi: 10.1002/chem.201700866. Epub 2017, Mar 23. PMID:28261912<ref>PMID:28261912</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6mfi" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Monteiro Pedroso | + | ==See Also== |
| - | [[Category: | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Simiduia agarivorans SA1 = DSM 21679]] | ||
| + | [[Category: Guddat L]] | ||
| + | [[Category: Monteiro Pedroso M]] | ||
| + | [[Category: Schenk G]] | ||
| + | [[Category: Selleck C]] | ||
Current revision
MIM-2 Metallo-Beta-Lactamase
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