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[[Image:4rhn.gif|left|200px]]


{{Structure
==HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH ADENOSINE==
|PDB= 4rhn |SIZE=350|CAPTION= <scene name='initialview01'>4rhn</scene>, resolution 1.90&Aring;
<StructureSection load='4rhn' size='340' side='right'caption='[[4rhn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=HIT:The+HIS+Triad+Forms+Part+Of+Alpha+Phosphate-Binding+Loop+...'>HIT</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=RIB:RIBOSE'>RIB</scene>
<table><tr><td colspan='2'>[[4rhn]] 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=4RHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RHN FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE= HINT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RIB:RIBOSE'>RIB</scene></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=4rhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rhn OCA], [https://pdbe.org/4rhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rhn RCSB], [https://www.ebi.ac.uk/pdbsum/4rhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rhn ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rh/4rhn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=4rhn ConSurf].
<div style="clear:both"></div>


'''HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH ADENOSINE'''
==See Also==
 
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
4RHN 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=4RHN OCA].
 
==Reference==
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]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Brenner C]]
[[Category: Brenner, C.]]
[[Category: Garrison P]]
[[Category: Garrison, P.]]
[[Category: Gilmour J]]
[[Category: Gilmour, J.]]
[[Category: Lowenstein JM]]
[[Category: Lowenstein, J M.]]
[[Category: Peisach D]]
[[Category: Peisach, D.]]
[[Category: Petsko GA]]
[[Category: Petsko, G A.]]
[[Category: Ringe D]]
[[Category: Ringe, D.]]
[[Category: RIB]]
[[Category: nucleotide-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:51 2008''
Retrieved from "https://proteopedia.org/4rhn"