1n07: Difference between revisions

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 <StructureSection load='1n07' size='340' side='right'caption='[[1n07]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N07 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N07 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N07 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n05|1n05]], [[1n06|1n06]], [[1n08|1n08]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPCC18.16C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=1n07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n07 OCA], [https://pdbe.org/1n07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n07 RCSB], [https://www.ebi.ac.uk/pdbsum/1n07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n07 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Riboflavin_kinase Riboflavin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.26 2.7.1.26] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n07 OCA], [http://pdbe.org/1n07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n07 RCSB], [http://www.ebi.ac.uk/pdbsum/1n07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n07 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RIFK_SCHPO RIFK_SCHPO]] Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
+[https://www.uniprot.org/uniprot/RIFK_SCHPO RIFK_SCHPO] Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n07 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-dependent riboflavin kinase and FAD synthetase. Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. The enzyme represents a novel family of phosphoryl transferring enzymes. It is a monomer comprising a central beta-barrel clasped on one side by two C-terminal helices that display an L-like shape. The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. Formation of the ATP-binding site requires significant rearrangements in a short alpha-helix as compared to the substrate free form. The diphosphate moiety of ADP is covered by the glycine-rich flap I formed from parts of this alpha-helix. In contrast, no significant changes are observed upon binding of riboflavin. The ribityl side-chain might be covered by a rather flexible flap II. The unusual metal-binding site involves, in addition to the ADP phosphates, only the strictly conserved Thr45. This may explain the preference for zinc observed in vitro.
-Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.,Bauer S, Kemter K, Bacher A, Huber R, Fischer M, Steinbacher S J Mol Biol. 2003 Mar 7;326(5):1463-73. PMID:12595258<ref>PMID:12595258</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n07" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Cbs 356]]
 [[Category: Large Structures]]
-[[Category: Riboflavin kinase]]
+[[Category: Schizosaccharomyces pombe]]
-[[Category: Bacher, A]]
+[[Category: Bacher A]]
-[[Category: Bauer, S]]
+[[Category: Bauer S]]
-[[Category: Fischer, M]]
+[[Category: Fischer M]]
-[[Category: Huber, R]]
+[[Category: Huber R]]
-[[Category: Kemter, K]]
+[[Category: Kemter K]]
-[[Category: Steinbacher, S]]
+[[Category: Steinbacher S]]
-[[Category: Flavin cofactor]]
-[[Category: Kinase]]
-[[Category: Metal binding]]
-[[Category: Phosphoryl transferase]]
-[[Category: Transferase]]