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==Crystal structure of PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI complexed with phosphate in active site==
==Crystal structure of PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI complexed with phosphate in active site==
<StructureSection load='4lef' size='340' side='right' caption='[[4lef]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='4lef' size='340' side='right'caption='[[4lef]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lef]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LEF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lef]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LEF FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.842&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bf6|1bf6]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lef RCSB], [http://www.ebi.ac.uk/pdbsum/4lef PDBsum]</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=4lef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lef OCA], [https://pdbe.org/4lef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lef RCSB], [https://www.ebi.ac.uk/pdbsum/4lef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lef ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHP_ECOLI PHP_ECOLI] Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: P-nitrophenyl acetate, L-alanine nitroanilide, P-nitrophenyl sulfate, bis(P-nitrophenyl) phosphate, paraoxon, and P-nitrophenyl phosphate. No enzymatic activity was detected with any of these nonspecific substrates.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Almo, S C.]]
[[Category: Escherichia coli K-12]]
[[Category: Fedorov, A A.]]
[[Category: Large Structures]]
[[Category: Fedorov, E V.]]
[[Category: Almo SC]]
[[Category: Raushel, F M.]]
[[Category: Fedorov AA]]
[[Category: Xiang, D F.]]
[[Category: Fedorov EV]]
[[Category: Hydrolase]]
[[Category: Raushel FM]]
[[Category: Php fold]]
[[Category: Xiang DF]]
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