1d2k

<StructureSection load='1d2k' size='340' side='right' caption='[[1d2k]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1d2k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cocit Cocit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D2K FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </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=1d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2k OCA], [http://pdbe.org/1d2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d2k RCSB], [http://www.ebi.ac.uk/pdbsum/1d2k PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/1d2k_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The X-ray structure of chitinase from the fungal pathogen Coccidioides immitis has been solved to 2.2 A resolution. Like other members of the class 18 hydrolase family, this 427 residue protein is an eight-stranded beta/alpha-barrel. Although lacking an N-terminal chitin anchoring domain, the enzyme closely resembles the chitinase from Serratia marcescens. Among the conserved features are three cis peptide bonds, all involving conserved active site residues. The active site is formed from conserved residues such as tryptophans 47, 131, 315, 378, tyrosines 239 and 293, and arginines 52 and 295. Glu171 is the catalytic acid in the hydrolytic mechanism; it was mutated to a Gln, and activity was abolished. Allosamidin is a substrate analog that strongly inhibits the class 18 enzymes. Its binding to the chitinase hevamine has been observed, and we used conserved structural features of the two enzymes to predict the inhibitors binding to the fungal enzyme.

The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis.,Hollis T, Monzingo AF, Bortone K, Ernst S, Cox R, Robertus JD Protein Sci. 2000 Mar;9(3):544-51. PMID:10752616<ref>PMID:10752616</ref>

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

</div>

<div class="pdbe-citations 1d2k" style="background-color:#fffaf0;"></div>

*[[Chitinase|Chitinase]]

[[Category: Chitinase]]

[[Category: Cocit]]

[[Category: Bortone, K]]

[[Category: Cox, R]]

[[Category: Ernst, S R]]

[[Category: Hollis, T]]

[[Category: Monzingo, A F]]

[[Category: Robertus, J D]]

[[Category: Hydrolase]]