4fll: Difference between revisions

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 ==Human MetAP1 with bengamide analog YZ6, in Mn form==
-<StructureSection load='4fll' size='340' side='right' caption='[[4fll]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='4fll' size='340' side='right'caption='[[4fll]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fll]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FLL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fll]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FLL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=YZ6:(E,2R,3R,4S,5R)-N-[(3R)-3-(FURAN-2-YL)-3-PHENYL-PROPYL]-2-METHOXY-8,8-DIMETHYL-3,4,5-TRIS(OXIDANYL)NON-6-ENAMIDE'>YZ6</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pka|3pka]], [[3pkb|3pkb]], [[3pkc|3pkc]], [[3pkd|3pkd]], [[3pke|3pke]], [[4fli|4fli]], [[4flj|4flj]], [[4flk|4flk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=YZ6:(E,2R,3R,4S,5R)-N-[(3R)-3-(FURAN-2-YL)-3-PHENYL-PROPYL]-2-METHOXY-8,8-DIMETHYL-3,4,5-TRIS(OXIDANYL)NON-6-ENAMIDE'>YZ6</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0094, map1, METAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fll OCA], [https://pdbe.org/4fll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fll RCSB], [https://www.ebi.ac.uk/pdbsum/4fll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fll ProSAT]</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=4fll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fll OCA], [http://pdbe.org/4fll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fll RCSB], [http://www.ebi.ac.uk/pdbsum/4fll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fll ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AMPM1_HUMAN AMPM1_HUMAN]] Removes the N-terminal methionine from nascent proteins. Required for normal progression through the cell cycle.<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
+[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] Cotranslationally 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). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Natural-product-derived bengamides possess potent antiproliferative activity and target human methionine aminopeptidases (MetAPs) for their cellular effects. Several derivatives were designed, synthesized, and evaluated as MetAP inhibitors. Here, we present four new X-ray structures of human MetAP1 in complex with the inhibitors. Together with the previous structures of bengamide derivatives with human MetAP2 and tubercular MtMetAP1c, analysis of the interactions of these inhibitors at the active site provides structural basis for further modification of these bengamide inhibitors for improved potency and selectivity as anticancer and antibacterial therapeutics.
-Structural Analysis of Bengamide Derivatives as Inhibitors of Methionine Aminopeptidases.,Xu W, Lu JP, Ye QZ J Med Chem. 2012 Sep 14. PMID:22913487<ref>PMID:22913487</ref>
+==See Also==
+*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4fll" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Methionyl aminopeptidase]]
+[[Category: Large Structures]]
-[[Category: Xu, W]]
+[[Category: Xu W]]
-[[Category: Ye, Q Z]]
+[[Category: Ye QZ]]
-[[Category: Enzyme-inhibitor complex]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]