1xcr

<StructureSection load='1xcr' size='340' side='right' caption='[[1xcr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1xcr]] 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=1XCR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XCR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DKFZp564H1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1xcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xcr OCA], [http://pdbe.org/1xcr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xcr RCSB], [http://www.ebi.ac.uk/pdbsum/1xcr PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CK054_HUMAN CK054_HUMAN]] Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.<ref>PMID:16522806</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xc/1xcr_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].

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== Publication Abstract from PubMed ==

The human protein PTD012 is the longer product of an alternatively spliced gene and was described to be localized in the nucleus. The X-ray structure analysis at 1.7 A resolution of PTD012 through SAD phasing reveals a monomeric protein and a novel fold. The shorter splice form was also studied and appears to be unfolded and non-functional. The structure of PTD012 displays an alphabetabetaalpha four-layer topology. A metal ion residing between the central beta-sheets is partially coordinated by three histidine residues. X-ray absorption near-edge structure (XANES) analysis identifies the PTD012-bound ion as Zn(2+). Tetrahedral coordination of the ion is completed by the carboxylate oxygen atom of an acetate molecule taken up from the crystallization buffer. The binding of Zn(2+) to PTD012 is reminiscent of zinc-containing enzymes such as carboxypeptidase, carbonic anhydrase, and beta-lactamase. Biochemical assays failed to demonstrate any of these enzyme activities in PTD012. However, PTD012 exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.

Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold.,Manjasetty BA, Bussow K, Fieber-Erdmann M, Roske Y, Gobom J, Scheich C, Gotz F, Niesen FH, Heinemann U Protein Sci. 2006 Apr;15(4):914-20. Epub 2006 Mar 7. PMID:16522806<ref>PMID:16522806</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 1xcr" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Buessow, K]]

[[Category: Fieber-Erdmann, M]]

[[Category: Goetz, F]]

[[Category: Heinemann, U]]

[[Category: Manjasetty, B A]]

[[Category: Roske, Y]]

[[Category: Zinc-containing fold]]