3f80

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{{STRUCTURE_3f80| PDB=3f80 | SCENE= }}
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==(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.==
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===(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.===
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<StructureSection load='3f80' size='340' side='right' caption='[[3f80]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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{{ABSTRACT_PUBMED_19032027}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3f80]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F80 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6HN:6-NITRO-L-NORLEUCINE'>6HN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>
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<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=3f80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f80 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f80 RCSB], [http://www.ebi.ac.uk/pdbsum/3f80 PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
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== Function ==
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==Disease==
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== Evolutionary Conservation ==
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[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref><ref>PMID:7649538</ref>
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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/f8/3f80_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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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The binding affinity of (S)-2-amino-6-nitrohexanoic acid to human arginase I was studied using surface plasmon resonance (K(d) = 60 microM), and the X-ray crystal structure of the enzyme-inhibitor complex was determined at 1.6 A resolution to reveal multiple nitro-metal coordination interactions.
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==About this Structure==
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(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster.,Zakharian TY, Di Costanzo L, Christianson DW J Am Chem Soc. 2008 Dec 24;130(51):17254-5. PMID:19032027<ref>PMID:19032027</ref>
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[[3f80]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F80 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:019032027</ref><references group="xtra"/><references/>
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</div>
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==See Also==
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*[[Arginase|Arginase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Christianson, D W.]]
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[[Category: Christianson, D W]]
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[[Category: Costanzo, L Di.]]
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[[Category: Costanzo, L Di]]
[[Category: Arginine metabolism]]
[[Category: Arginine metabolism]]
[[Category: Disease mutation]]
[[Category: Disease mutation]]

Revision as of 13:09, 18 December 2014

(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.

3f80, resolution 1.60Å

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