4z7m
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Novel Inhibitors of Bacterial Methionine Aminopeptidase with Broad-Spectrum Biochemical Activity== | |
| - | + | <StructureSection load='4z7m' size='340' side='right' caption='[[4z7m]], [[Resolution|resolution]] 1.43Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4z7m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z7M FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4L9:N~2~-[(3,5-DIFLUOROPHENYL)ACETYL]-N-[(3S,7R)-1-METHYL-2-OXO-7-PHENYL-2,3,4,7-TETRAHYDRO-1H-AZEPIN-3-YL]-L-ALANINAMIDE'>4L9</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr> |
| - | [[Category: | + | <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=4z7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7m OCA], [http://pdbe.org/4z7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z7m RCSB], [http://www.ebi.ac.uk/pdbsum/4z7m PDBsum]</span></td></tr> |
| - | [[Category: Fleming, P | + | </table> |
| - | [[Category: Lahiri, S | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/MAP1_ECO57 MAP1_ECO57]] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Methionyl aminopeptidase]] | ||
| + | [[Category: Albert, R]] | ||
| + | [[Category: Fisher, S F]] | ||
| + | [[Category: Fleming, P R]] | ||
| + | [[Category: Lahiri, S D]] | ||
| + | [[Category: McKinney, D C]] | ||
[[Category: Morningstar, M]] | [[Category: Morningstar, M]] | ||
| - | [[Category: Rose, J | + | [[Category: Rose, J A]] |
| - | [[Category: | + | [[Category: Shapiro, A B]] |
| - | [[Category: | + | [[Category: Antibacterial]] |
| + | [[Category: Azepinone]] | ||
| + | [[Category: Drug discovery]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Methionine aminopeptidase]] | ||
| + | [[Category: Structure-based design]] | ||
Revision as of 11:21, 12 May 2016
Novel Inhibitors of Bacterial Methionine Aminopeptidase with Broad-Spectrum Biochemical Activity
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