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==HsMetAP (F220M) in complex with 1-amino-2-propylpentyl]phosphonic acid==
==HsMetAP (F220M) in complex with 1-amino-2-propylpentyl]phosphonic acid==
<StructureSection load='4u6w' size='340' side='right' caption='[[4u6w]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='4u6w' size='340' side='right'caption='[[4u6w]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4u6w]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6W FirstGlance]. <br>
<table><tr><td colspan='2'>[[4u6w]] 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=4U6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U6W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=Q08:[(1R)-1-AMINO-2-PROPYLPENTYL]PHOSPHONIC+ACID'>Q08</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]] 1.83&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1b|4u1b]], [[4u69|4u69]], [[4u6c|4u6c]], [[4u6e|4u6e]], [[4u6j|4u6j]], [[4u6z|4u6z]], [[4u70|4u70]], [[4u71|4u71]], [[4u73|4u73]], [[4u75|4u75]], [[4u76|4u76]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=Q08:[(1R)-1-AMINO-2-PROPYLPENTYL]PHOSPHONIC+ACID'>Q08</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4u6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6w OCA], [https://pdbe.org/4u6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u6w RCSB], [https://www.ebi.ac.uk/pdbsum/4u6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6w ProSAT]</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=4u6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6w OCA], [http://pdbe.org/4u6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6w RCSB], [http://www.ebi.ac.uk/pdbsum/4u6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u6w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4u6w" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4u6w" style="background-color:#fffaf0;"></div>
==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Methionyl aminopeptidase]]
[[Category: Homo sapiens]]
[[Category: Addlagatta, A]]
[[Category: Large Structures]]
[[Category: Arya, T]]
[[Category: Addlagatta A]]
[[Category: Hydrolase]]
[[Category: Arya T]]
[[Category: Inhibitor complex]]