This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5mj6
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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.== | ||
| - | <StructureSection load='5mj6' size='340' side='right' caption='[[5mj6]], [[Resolution|resolution]] 2.53Å' scene=''> | + | <StructureSection load='5mj6' size='340' side='right'caption='[[5mj6]], [[Resolution|resolution]] 2.53Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <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:// | + | <table><tr><td colspan='2'>[[5mj6]] is a 2 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=5MJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MJ6 FirstGlance]. <br> |
| - | </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= | + | </td></tr><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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LNPEP, OTASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<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> | <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> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> |
</table> | </table> | ||
== Function == | == Function == | ||
| Line 19: | Line 20: | ||
</div> | </div> | ||
<div class="pdbe-citations 5mj6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5mj6" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 24: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cystinyl aminopeptidase]] | [[Category: Cystinyl aminopeptidase]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Giastas, P]] | [[Category: Giastas, P]] | ||
[[Category: Mpakali, A]] | [[Category: Mpakali, A]] | ||
Revision as of 07:20, 19 August 2020
Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.
| |||||||||||
Categories: Cystinyl aminopeptidase | Human | Large Structures | Giastas, P | Mpakali, A | Saridakis, E | Stratikos, E | Endoplasmatic reticulum aminopeptidase | Generation of antigenic peptides for cross-presentation | Hydrolase | Insulin-regulated aminopeptidase | Ligand-induced conformational change | Phosphinic pseudotripeptide
