2adu

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<StructureSection load='2adu' size='340' side='right'caption='[[2adu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2adu' size='340' side='right'caption='[[2adu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2adu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2adu]] 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=2ADU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=R20:4-(3-METHYLPHENYL)-1H-1,2,3-TRIAZOLE'>R20</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">METAP2, MNPEP, P67EIF2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=R20:4-(3-METHYLPHENYL)-1H-1,2,3-TRIAZOLE'>R20</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2adu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adu OCA], [https://pdbe.org/2adu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adu RCSB], [https://www.ebi.ac.uk/pdbsum/2adu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adu ProSAT]</span></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=2adu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adu OCA], [https://pdbe.org/2adu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adu RCSB], [https://www.ebi.ac.uk/pdbsum/2adu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AMPM2_HUMAN AMPM2_HUMAN]] Removes the N-terminal methionine from nascent proteins. The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.<ref>PMID:2511207</ref> <ref>PMID:20521764</ref> <ref>PMID:14534293</ref> <ref>PMID:17636946</ref> Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.<ref>PMID:2511207</ref> <ref>PMID:20521764</ref> <ref>PMID:14534293</ref> <ref>PMID:17636946</ref>
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[https://www.uniprot.org/uniprot/MAP2_HUMAN MAP2_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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2adu_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/2adu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Methionyl aminopeptidase]]
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[[Category: Chen W]]
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[[Category: Chen, W]]
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[[Category: Fisher PW]]
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[[Category: Fisher, P W]]
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[[Category: Hansbury MJ]]
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[[Category: Hansbury, M J]]
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[[Category: Ho TF]]
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[[Category: Ho, T F]]
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[[Category: Hofmann GA]]
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[[Category: Hofmann, G A]]
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[[Category: Janson CA]]
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[[Category: Janson, C A]]
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[[Category: Johanson KO]]
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[[Category: Johanson, K O]]
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[[Category: Johnson RK]]
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[[Category: Johnson, R K]]
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[[Category: Kallander LS]]
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[[Category: Kallander, L S]]
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[[Category: Kirkpatrick RB]]
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[[Category: Kirkpatrick, R B]]
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[[Category: Lu Q]]
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[[Category: Lu, Q]]
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[[Category: Mattern MR]]
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[[Category: Mattern, M R]]
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[[Category: Meek TD]]
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[[Category: Meek, T D]]
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[[Category: Ryan MD]]
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[[Category: Ryan, M D]]
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[[Category: Schulz-Pritchard CK]]
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[[Category: Schulz-Pritchard, C K]]
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[[Category: Smith WW]]
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[[Category: Smith, W W]]
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[[Category: Tew D]]
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[[Category: Tew, D]]
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[[Category: Thompson SK]]
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[[Category: Thompson, S K]]
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[[Category: Tomaszek T]]
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[[Category: Tomaszek, T]]
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[[Category: Veber DF]]
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[[Category: Veber, D F]]
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[[Category: Ward KW]]
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[[Category: Ward, K W]]
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[[Category: Winkler JD]]
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[[Category: Winkler, J D]]
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[[Category: Yang G]]
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[[Category: Yang, G]]
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[[Category: Zhang GF]]
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[[Category: Zhang, G F]]
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[[Category: Aminopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Metal binding]]
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[[Category: Protease]]
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Current revision

Human Methionine Aminopeptidase Complex with 4-Aryl-1,2,3-triazole Inhibitor

PDB ID 2adu

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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