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5mj6

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==Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.==
==Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.==
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<StructureSection load='5mj6' size='340' side='right' caption='[[5mj6]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
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<StructureSection load='5mj6' size='340' side='right'caption='[[5mj6]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mj6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MJ6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mj6]] is a 2 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=5MJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MJ6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7O2:[(2~{S})-2-[[(2~{S})-1-AZANYL-1-OXIDANYLIDENE-3-PHENYL-PROPAN-2-YL]CARBAMOYL]-4,4-DIPHENYL-BUTYL]-[(1~{R})-1-AZANYL-3-PHENYL-PROPYL]PHOSPHINIC+ACID'>7O2</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.53&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystinyl_aminopeptidase Cystinyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.3 3.4.11.3] </span></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=7O2:[(2~{S})-2-[[(2~{S})-1-AZANYL-1-OXIDANYLIDENE-3-PHENYL-PROPAN-2-YL]CARBAMOYL]-4,4-DIPHENYL-BUTYL]-[(1~{R})-1-AZANYL-3-PHENYL-PROPYL]PHOSPHINIC+ACID'>7O2</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=5mj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mj6 OCA], [http://pdbe.org/5mj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mj6 RCSB], [http://www.ebi.ac.uk/pdbsum/5mj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mj6 ProSAT]</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=5mj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mj6 OCA], [https://pdbe.org/5mj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mj6 RCSB], [https://www.ebi.ac.uk/pdbsum/5mj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mj6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LCAP_HUMAN LCAP_HUMAN]] Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.<ref>PMID:11389728</ref> <ref>PMID:11707427</ref> <ref>PMID:1731608</ref>
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[https://www.uniprot.org/uniprot/LCAP_HUMAN LCAP_HUMAN] Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.<ref>PMID:11389728</ref> <ref>PMID:11707427</ref> <ref>PMID:1731608</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 5mj6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5mj6" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cystinyl aminopeptidase]]
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[[Category: Homo sapiens]]
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[[Category: Giastas, P]]
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[[Category: Large Structures]]
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[[Category: Mpakali, A]]
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[[Category: Giastas P]]
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[[Category: Saridakis, E]]
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[[Category: Mpakali A]]
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[[Category: Stratikos, E]]
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[[Category: Saridakis E]]
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[[Category: Endoplasmatic reticulum aminopeptidase]]
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[[Category: Stratikos E]]
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[[Category: Generation of antigenic peptides for cross-presentation]]
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[[Category: Hydrolase]]
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[[Category: Insulin-regulated aminopeptidase]]
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[[Category: Ligand-induced conformational change]]
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[[Category: Phosphinic pseudotripeptide]]
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Current revision

Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.

PDB ID 5mj6

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