2rks

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[[Image:2rks.png|left|200px]]
 
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{{STRUCTURE_2rks| PDB=2rks | SCENE= }}
{{STRUCTURE_2rks| PDB=2rks | SCENE= }}
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===Crystal structure of Staphylococcal nuclease variant PHS L38K at cryogenic temperature===
===Crystal structure of Staphylococcal nuclease variant PHS L38K at cryogenic temperature===
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{{ABSTRACT_PUBMED_18369193}}
{{ABSTRACT_PUBMED_18369193}}
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==Function==
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[[http://www.uniprot.org/uniprot/NUC_STAAW NUC_STAAW]] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond (By similarity).
==About this Structure==
==About this Structure==
[[2rks]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKS OCA].
[[2rks]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKS OCA].
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==See Also==
 
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*[[Staphylococcal nuclease|Staphylococcal nuclease]]
 
==Reference==
==Reference==
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<ref group="xtra">PMID:018369193</ref><references group="xtra"/>
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<ref group="xtra">PMID:018369193</ref><references group="xtra"/><references/>
[[Category: Micrococcal nuclease]]
[[Category: Micrococcal nuclease]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]

Revision as of 07:25, 30 June 2013

Template:STRUCTURE 2rks

Contents

Crystal structure of Staphylococcal nuclease variant PHS L38K at cryogenic temperature

Template:ABSTRACT PUBMED 18369193

Function

[NUC_STAAW] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond (By similarity).

About this Structure

2rks is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

  • Harms MJ, Schlessman JL, Chimenti MS, Sue GR, Damjanovic A, Garcia-Moreno B. A buried lysine that titrates with a normal pKa: role of conformational flexibility at the protein-water interface as a determinant of pKa values. Protein Sci. 2008 May;17(5):833-45. Epub 2008 Mar 27. PMID:18369193 doi:10.1110/ps.073397708

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