1h8v: Difference between revisions

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 <StructureSection load='1h8v' size='340' side='right'caption='[[1h8v]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h8v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h8v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8V FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oa2|1oa2]], [[1olq|1olq]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8v OCA], [https://pdbe.org/1h8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8v RCSB], [https://www.ebi.ac.uk/pdbsum/1h8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8v ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O00095_HYPJE O00095_HYPJE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 20: @@
 </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/main_output.php?pdb_ID=1h8v ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We present the three-dimensional structure of Trichoderma reesei endoglucanase 3 (Cel12A), a small, 218 amino acid residue (24.5 kDa), neutral pI, glycoside hydrolase family 12 cellulase that lacks a cellulose-binding module. The structure has been determined using X-ray crystallography and refined to 1.9 A resolution. The asymmetric unit consists of six non-crystallographic symmetry-related molecules that were exploited to improve initial multiple isomorphous replacement phasing, and subsequent structure refinement. The enzyme contains one disulfide bridge and is glycosylated at Asp164 by a single N-acetyl glucosamine residue. The protein has the expected fold for a glycoside hydrolase clan-C family 12 enzyme. It contains two beta-sheets, of six and nine strands, packed on top of one another, and one alpha-helix. The concave surface of the nine-stranded beta-sheet forms a large substrate-binding groove in which the active-site residues are located. In the active site, we find a carboxylic acid trio, similar to that of glycoside hydrolase families 7 and 16. The strictly conserved Asp99 hydrogen bonds to the nucleophile, the invariant Glu116. The binding crevice is lined with both aromatic and polar amino acid side-chains which may play a role in substrate binding. The structure of the fungal family 12 enzyme presented here allows a complete structural characterization of the glycoside hydrolase-C clan.
-The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution.,Sandgren M, Shaw A, Ropp TH, Wu S, Bott R, Cameron AD, Stahlberg J, Mitchinson C, Jones TA J Mol Biol. 2001 Apr 27;308(2):295-310. PMID:11327768<ref>PMID:11327768</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1h8v" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Glucanase 3D structures|Glucanase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 13631]]
-[[Category: Cellulase]]
 [[Category: Large Structures]]
-[[Category: Bott, R]]
+[[Category: Trichoderma reesei]]
-[[Category: Cameron, A D]]
+[[Category: Bott R]]
-[[Category: Jones, T A]]
+[[Category: Cameron AD]]
-[[Category: Mitchinson, C]]
+[[Category: Jones TA]]
-[[Category: Ropp, T H]]
+[[Category: Mitchinson C]]
-[[Category: Sandgren, M]]
+[[Category: Ropp TH]]
-[[Category: Shaw, A]]
+[[Category: Sandgren M]]
-[[Category: Stahlberg, J]]
+[[Category: Shaw A]]
-[[Category: Wu, S]]
+[[Category: Stahlberg J]]
-[[Category: Cellulose degradation]]
+[[Category: Wu S]]
-[[Category: Gh family 12]]
-[[Category: Glycosyl hydrolase]]
-[[Category: Hydrolase]]