4do7: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4do7 is ON HOLD
+==Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2==
+<StructureSection load='4do7' size='340' side='right'caption='[[4do7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-Authors: Vetting, M.W., Toro, R., Bhosle, R., Wasserman, S.R., Morisco, L.L., Sojitra, S., Seidel, R.D., Hillerich, B., Washington, E., Scott Glenn, A., Chowdhury, S., Evans, B., Hammonds, J., Al Obaidi, N.F., Zencheck, W.D., Imker, H.J., Gerlt, J.A., Raushel, F.M., Almo, S.C., Enzyme Function Initiative (EFI)
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4do7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_multivorans_ATCC_17616 Burkholderia multivorans ATCC 17616]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DO7 FirstGlance]. <br>
-Description: CRYSTAL STRUCTURE OF AN AMIDOHYDROLASE (COG3618) FROM BURKHOLDERIA MULTIVORANS (TARGET EFI-500235) WITH BOUND ZN, SPACE GROUP C2
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4do7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do7 OCA], [https://pdbe.org/4do7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do7 RCSB], [https://www.ebi.ac.uk/pdbsum/4do7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FCNLN_BURM1 FCNLN_BURM1] L-fucono-1,5-lactonase involved in an L-fucose degradation pathway (PubMed:23214453). Catalyzes the hydrolysis of L-fucono-1,5-lactone to L-fuconate (PubMed:23214453). L-fucono-1,5-lactone is the best substrate, but the enzyme can also hydrolyze L-fucono-1,4-lactone, L-galactono-1,4-lactone D-arabinono-1,4-lactone and L-xylono-1,4-lactone (PubMed:23214453).<ref>PMID:23214453</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Burkholderia multivorans ATCC 17616]]
+[[Category: Large Structures]]
+[[Category: Al Obaidi NF]]
+[[Category: Almo SC]]
+[[Category: Bhosle R]]
+[[Category: Chowdhury S]]
+[[Category: Evans B]]
+[[Category: Gerlt JA]]
+[[Category: Hammonds J]]
+[[Category: Hillerich B]]
+[[Category: Imker HJ]]
+[[Category: Morisco LL]]
+[[Category: Raushel FM]]
+[[Category: Scott Glenn A]]
+[[Category: Seidel RD]]
+[[Category: Sojitra S]]
+[[Category: Toro R]]
+[[Category: Vetting MW]]
+[[Category: Washington E]]
+[[Category: Wasserman SR]]
+[[Category: Zencheck WD]]