4i9d: Difference between revisions
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==X-ray structure of NikA in complex with Fe-N,N'-Bis(2-pyridylmethyl)-N-carboxymethyl-N'-methyl== | |||
<StructureSection load='4i9d' size='340' side='right' caption='[[4i9d]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4i9d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I9D FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=L4D:{(S)-N-(2-{METHYL[(PYRIDIN-2-YL-KAPPAN)METHYL]AMINO-KAPPAN}ETHYL)-N-[(PYRIDIN-2-YL-KAPPAN)METHYL]GLYCINATO-KAPPA~2~N,O}IRON(2+)'>L4D</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dcx|4dcx]], [[4dcy|4dcy]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3476, JW3441, nikA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 ECOBD])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nickel-transporting_ATPase Nickel-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.24 3.6.3.24] </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=4i9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i9d OCA], [http://pdbe.org/4i9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i9d RCSB], [http://www.ebi.ac.uk/pdbsum/4i9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i9d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NIKA_ECOLI NIKA_ECOLI]] Involved in a nickel transport system, probably represents the nickel binder. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The substrate for an artificial iron monooxygenase was selected by using docking calculations. The high catalytic efficiency of the reported enzyme for sulfide oxidation was directly correlated to the predicted substrate binding mode in the protein cavity, thus illustrating the synergetic effect of the substrate binding site, protein scaffold, and catalytic site. | |||
An artificial oxygenase built from scratch: substrate binding site identified using a docking approach.,Esmieu C, Cherrier MV, Amara P, Girgenti E, Marchi-Delapierre C, Oddon F, Iannello M, Jorge-Robin A, Cavazza C, Menage S Angew Chem Int Ed Engl. 2013 Apr 2;52(14):3922-5. doi: 10.1002/anie.201209021., Epub 2013 Feb 25. PMID:23440925<ref>PMID:23440925</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4i9d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ecobd]] | |||
[[Category: Nickel-transporting ATPase]] | |||
[[Category: Amara, P]] | |||
[[Category: Cavazza, C]] | |||
[[Category: Cherrier, M V]] | |||
[[Category: Iannello, M]] | |||
[[Category: Metal transport]] | |||
[[Category: Protein-bound iron complex]] | |||
[[Category: Transport protein]] | |||
Latest revision as of 21:40, 11 August 2016
X-ray structure of NikA in complex with Fe-N,N'-Bis(2-pyridylmethyl)-N-carboxymethyl-N'-methylX-ray structure of NikA in complex with Fe-N,N'-Bis(2-pyridylmethyl)-N-carboxymethyl-N'-methyl
Structural highlights
Function[NIKA_ECOLI] Involved in a nickel transport system, probably represents the nickel binder. Publication Abstract from PubMedThe substrate for an artificial iron monooxygenase was selected by using docking calculations. The high catalytic efficiency of the reported enzyme for sulfide oxidation was directly correlated to the predicted substrate binding mode in the protein cavity, thus illustrating the synergetic effect of the substrate binding site, protein scaffold, and catalytic site. An artificial oxygenase built from scratch: substrate binding site identified using a docking approach.,Esmieu C, Cherrier MV, Amara P, Girgenti E, Marchi-Delapierre C, Oddon F, Iannello M, Jorge-Robin A, Cavazza C, Menage S Angew Chem Int Ed Engl. 2013 Apr 2;52(14):3922-5. doi: 10.1002/anie.201209021., Epub 2013 Feb 25. PMID:23440925[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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