1h5s: Difference between revisions

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[[Image:1h5s.gif|left|200px]]<br /><applet load="1h5s" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1h5s.gif|left|200px]]
caption="1h5s, resolution 2.3&Aring;" />
 
'''THYMIDYLYLTRANSFERASE COMPLEXED WITH TMP'''<br />
{{Structure
|PDB= 1h5s |SIZE=350|CAPTION= <scene name='initialview01'>1h5s</scene>, resolution 2.3&Aring;
|SITE= <scene name='pdbsite=AC1:Tmp+Binding+Site+For+Chain+D'>AC1</scene>
|LIGAND= <scene name='pdbligand=TMP:THYMIDINE-5'-PHOSPHATE'>TMP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24]
|GENE=
}}
 
'''THYMIDYLYLTRANSFERASE COMPLEXED WITH TMP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1H5S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=TMP:'>TMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] Known structural/functional Site: <scene name='pdbsite=AC1:Tmp+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5S OCA].  
1H5S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5S OCA].  


==Reference==
==Reference==
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11697907 11697907]
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11697907 11697907]
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: transferase]]
[[Category: transferase]]


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