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<StructureSection load='3tw2' size='340' side='right'caption='[[3tw2]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
<StructureSection load='3tw2' size='340' side='right'caption='[[3tw2]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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]] 1.38&#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;'>[[1av5|1av5]], [[1kpe|1kpe]], [[1kpf|1kpf]], [[1kpa|1kpa]], [[1kpb|1kpb]], [[1kpc|1kpc]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HINT1, HINT, PKCI1, PRKCNH1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3tw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw2 OCA], [https://pdbe.org/3tw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw2 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw2 ProSAT]</span></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=3tw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw2 OCA], [https://pdbe.org/3tw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw2 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HINT1_HUMAN HINT1_HUMAN]] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity).  
[https://www.uniprot.org/uniprot/HINT1_HUMAN HINT1_HUMAN] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch of the histidine triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the structure of the human HINT1-adenosine 5'-monophosphate (AMP) complex at 1.38 A resolution obtained from a new monoclinic crystal form is reported. The final structure has R(cryst) = 0.1207 (R(free) = 0.1615) and the model exhibits good stereochemical quality. Detailed analysis of the high-resolution data allowed the details of the protein structure to be updated in comparison to the previously published data.
 
A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 A resolution.,Dolot R, Ozga M, Wlodarczyk A, Krakowiak A, Nawrot B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Aug;68(Pt 8):883-8. Epub, 2012 Jul 27. PMID:22869114<ref>PMID:22869114</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tw2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dolot, R M]]
[[Category: Dolot RM]]
[[Category: Krakowiak, A]]
[[Category: Krakowiak A]]
[[Category: Nawrot, B]]
[[Category: Nawrot B]]
[[Category: Ozga, M]]
[[Category: Ozga M]]
[[Category: Wlodarczyk, A]]
[[Category: Wlodarczyk A]]
[[Category: Hydrolase]]
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