1x2e: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1x2e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X2E FirstGlance]. <br> | <table><tr><td colspan='2'>[[1x2e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X2E FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATX:(2S)-2-AMINO-1-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)PROPAN-1-ONE'>ATX</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATX:(2S)-2-AMINO-1-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)PROPAN-1-ONE'>ATX</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qtr|1qtr]], [[1wm1|1wm1]], [[1x2b|1x2b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qtr|1qtr]], [[1wm1|1wm1]], [[1x2b|1x2b]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x2e RCSB], [http://www.ebi.ac.uk/pdbsum/1x2e PDBsum]</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=1x2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x2e RCSB], [http://www.ebi.ac.uk/pdbsum/1x2e PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PIP_SERMA PIP_SERMA]] Specifically catalyzes the removal of N-terminal proline residues from peptides. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Hatakeyama, S | [[Category: Hatakeyama, S]] | ||
[[Category: Ito, K | [[Category: Ito, K]] | ||
[[Category: Matsubara, F | [[Category: Matsubara, F]] | ||
[[Category: Nakajima, Y | [[Category: Nakajima, Y]] | ||
[[Category: Sakata, M | [[Category: Sakata, M]] | ||
[[Category: Xu, Y | [[Category: Xu, Y]] | ||
[[Category: Yoshimoto, T | [[Category: Yoshimoto, T]] | ||
[[Category: Alpha/beta-hydrolase fold]] | [[Category: Alpha/beta-hydrolase fold]] | ||
[[Category: Binary complex]] | [[Category: Binary complex]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Prolyl iminopeptidase]] | [[Category: Prolyl iminopeptidase]] | ||