1ot5

<table><tr><td colspan='2'>[[1ot5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OT5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BOR:(1R)-1-AMINO-4-{[(E)-AMINO(IMINO)METHYL]AMINO}BUTYLBORONIC+ACID'>BOR</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KEX2 OR QDS1 OR YNL238W OR N1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ot5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot5 OCA], [http://pdbe.org/1ot5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ot5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ot5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/KEX2_YEAST KEX2_YEAST]] Processing of precursors of alpha-factors and killer toxin.

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== Publication Abstract from PubMed ==

This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine.

2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor.,Holyoak T, Wilson MA, Fenn TD, Kettner CA, Petsko GA, Fuller RS, Ringe D Biochemistry. 2003 Jun 10;42(22):6709-18. PMID:12779325<ref>PMID:12779325</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ot5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Kexin]]

[[Category: Fenn, T D]]

[[Category: Fuller, R S]]

[[Category: Holyoak, T]]

[[Category: Kettner, C A]]

[[Category: Petsko, G A]]

[[Category: Ringe, D]]

[[Category: Wilson, M A]]

[[Category: Subtilisin fold]]