4z7m
From Proteopedia
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==Novel Inhibitors of Bacterial Methionine Aminopeptidase with Broad-Spectrum Biochemical Activity== | ==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=''> | + | <StructureSection load='4z7m' size='340' side='right'caption='[[4z7m]], [[Resolution|resolution]] 1.43Å' scene=''> |
== Structural highlights == | == 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> | + | <table><tr><td colspan='2'>[[4z7m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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> | </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> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">map, Z0178, ECs0170 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<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> | <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> | ||
| - | <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> | + | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z7m ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[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. | [[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. | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
[[Category: Albert, R]] | [[Category: Albert, R]] | ||
Revision as of 06:47, 19 June 2019
Novel Inhibitors of Bacterial Methionine Aminopeptidase with Broad-Spectrum Biochemical Activity
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Categories: Bacillus coli migula 1895 | Large Structures | Methionyl aminopeptidase | Albert, R | Fisher, S F | Fleming, P R | Lahiri, S D | McKinney, D C | Morningstar, M | Rose, J A | Shapiro, A B | Antibacterial | Azepinone | Drug discovery | Hydrolase-hydrolase inhibitor complex | Methionine aminopeptidase | Structure-based design
