4lef
From Proteopedia
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<StructureSection load='4lef' size='340' side='right'caption='[[4lef]], [[Resolution|resolution]] 1.84Å' scene=''> | <StructureSection load='4lef' size='340' side='right'caption='[[4lef]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4lef]] is a 8 chain structure with sequence from [ | + | <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 id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.842Å</td></tr> |
| - | <tr id=' | + | <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 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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Fedorov | + | [[Category: Fedorov AA]] |
| - | [[Category: Fedorov | + | [[Category: Fedorov EV]] |
| - | [[Category: Raushel | + | [[Category: Raushel FM]] |
| - | [[Category: Xiang | + | [[Category: Xiang DF]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of PHOSPHOTRIESTERASE HOMOLOGY PROTEIN FROM ESCHERICHIA COLI complexed with phosphate in active site
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