3rhn

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[[Image:3rhn.png|left|200px]]
 
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{{STRUCTURE_3rhn| PDB=3rhn | SCENE= }}
{{STRUCTURE_3rhn| PDB=3rhn | SCENE= }}
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===HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP===
===HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH GMP===
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{{ABSTRACT_PUBMED_9164465}}
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==Function==
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[[http://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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{{ABSTRACT_PUBMED_9164465}}
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==About this Structure==
==About this Structure==
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3RHN is a 1 chain 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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[[3rhn]] is a 1 chain structure with 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].
==Reference==
==Reference==
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<ref group="xtra">PMID:9164465</ref><references group="xtra"/>
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<ref group="xtra">PMID:009164465</ref><references group="xtra"/><references/>
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Brenner, C.]]
[[Category: Brenner, C.]]
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[[Category: Histidine]]
[[Category: Histidine]]
[[Category: Nucleotide-binding protein]]
[[Category: Nucleotide-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:56:40 2009''
 

Revision as of 08:12, 16 May 2013

Template:STRUCTURE 3rhn

Contents

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

Template:ABSTRACT PUBMED 9164465

Function

[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.

About this Structure

3rhn is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

  • Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat Struct Biol. 1997 Mar;4(3):231-8. PMID:9164465

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