1hjk: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==ALKALINE PHOSPHATASE MUTANT H331Q== | ==ALKALINE PHOSPHATASE MUTANT H331Q== | ||
<StructureSection load='1hjk' size='340' side='right' caption='[[1hjk]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1hjk' size='340' side='right' caption='[[1hjk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| Line 7: | Line 8: | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] </span></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=1hjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjk OCA], [http://pdbe.org/1hjk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hjk RCSB], [http://www.ebi.ac.uk/pdbsum/1hjk PDBsum]</span></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=1hjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjk OCA], [http://pdbe.org/1hjk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hjk RCSB], [http://www.ebi.ac.uk/pdbsum/1hjk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 13: | Line 14: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hjk_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hjk_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 28: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 1hjk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1hjk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:35, 10 January 2018
ALKALINE PHOSPHATASE MUTANT H331QALKALINE PHOSPHATASE MUTANT H331Q
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUsing a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate. Trapping and visualization of a covalent enzyme-phosphate intermediate.,Murphy JE, Stec B, Ma L, Kantrowitz ER Nat Struct Biol. 1997 Aug;4(8):618-22. PMID:9253408[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||||||||