3fe5

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[[Image:3fe5.png|left|200px]]
 
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==Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney==
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The line below this paragraph, containing "STRUCTURE_3fe5", creates the "Structure Box" on the page.
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<StructureSection load='3fe5' size='340' side='right'caption='[[3fe5]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fe5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FE5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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{{STRUCTURE_3fe5| PDB=3fe5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fe5 OCA], [https://pdbe.org/3fe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fe5 RCSB], [https://www.ebi.ac.uk/pdbsum/3fe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fe5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/3HAO_BOVIN 3HAO_BOVIN] Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate (By similarity).[HAMAP-Rule:MF_03019]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/3fe5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3fe5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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3-Hydroxyanthranilate 3,4-dioxygenase, the enzyme that catalyzes the conversion of 3-hydroxyanthranilate to quinolinic acid, has been extracted and purified from bovine kidney, crystallized and its structure determined at 2.5 A resolution. The enzyme, which crystallizes in the triclinic P1 space group, is a monomer, characterized by the so-called cupin fold. The monomer of the bovine enzyme mimics the dimer present in lower species, such as bacteria and yeast, since it is composed of two domains: one of them is equivalent to one monomer, whilst the second domain corresponds to only a portion of it. The active site consists of an iron ion coordinated by two histidine residues, one glutamate and an external ligand, which has been interpreted as a solvent molecule. It is contained in the N-terminal domain, whilst the function of the C-terminal domain is possibly structural. The catalytic mechanism very likely has been conserved through all species, since the positions of all residues considered relevant for the reaction are present from bacteria to humans. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009.
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===Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney===
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Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase.,Dilovic I, Gliubich F, Malpeli G, Zanotti G, Matkovic-Calogovic D Biopolymers. 2009 Feb 18. PMID:19226621<ref>PMID:19226621</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3fe5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19226621}}, adds the Publication Abstract to the page
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19226621 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19226621}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3fe5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FE5 OCA].
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==Reference==
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<ref group="xtra">PMID:19226621</ref><ref group="xtra">PMID:15909978</ref><ref group="xtra">PMID:16522801</ref><references group="xtra"/>
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[[Category: 3-hydroxyanthranilate 3,4-dioxygenase]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Dilovic, I.]]
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[[Category: Large Structures]]
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[[Category: Gliubich, F.]]
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[[Category: Dilovic I]]
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[[Category: Malpeli, G.]]
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[[Category: Gliubich F]]
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[[Category: Matkovic-Calogovic, D.]]
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[[Category: Malpeli G]]
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[[Category: Zanotti, G.]]
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[[Category: Matkovic-Calogovic D]]
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[[Category: 3hao]]
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[[Category: Zanotti G]]
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[[Category: Cupin]]
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[[Category: Cytoplasm]]
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[[Category: Dioxygenase]]
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[[Category: Iron]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Quinolinic acid]]
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Current revision

Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney

PDB ID 3fe5

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