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3rhn

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[[Image:3rhn.jpg|left|200px]]
 
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{{Structure
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==HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP==
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|PDB= 3rhn |SIZE=350|CAPTION= <scene name='initialview01'>3rhn</scene>, resolution 2.10&Aring;
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<StructureSection load='3rhn' size='340' side='right'caption='[[3rhn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=HIT:The+HIS+Triad+Forms+Part+Of+Alpha+Phosphate-Binding+Loop+...'>HIT</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=5GP:GUANOSINE-5&#39;-MONOPHOSPHATE'>5GP</scene>
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<table><tr><td colspan='2'>[[3rhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RHN FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.1&#8491;</td></tr>
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|GENE= HINT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene></td></tr>
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}}
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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=3rhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rhn OCA], [https://pdbe.org/3rhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rhn RCSB], [https://www.ebi.ac.uk/pdbsum/3rhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rhn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HINT1_RABIT HINT1_RABIT] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
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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/rh/3rhn_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/main_output.php?pdb_ID=3rhn ConSurf].
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<div style="clear:both"></div>
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'''HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP'''
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==See Also==
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*[[Histidine triad nucleotide-binding protein|Histidine triad nucleotide-binding protein]]
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*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
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==Overview==
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__TOC__
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Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.
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</StructureSection>
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[[Category: Large Structures]]
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==About this Structure==
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3RHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RHN OCA].
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==Reference==
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Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins., Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM, Nat Struct Biol. 1997 Mar;4(3):231-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9164465 9164465]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Brenner C]]
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[[Category: Brenner, C.]]
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[[Category: Garrison P]]
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[[Category: Garrison, P.]]
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[[Category: Gilmour J]]
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[[Category: Gilmour, J.]]
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[[Category: Lowenstein JM]]
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[[Category: Lowenstein, J M.]]
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[[Category: Peisach D]]
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[[Category: Peisach, D.]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G A.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: 5GP]]
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[[Category: histidine]]
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[[Category: nucleotide-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 16:03:20 2008''
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Current revision

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP

PDB ID 3rhn

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