1d5h: Difference between revisions

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{{Seed}}
[[Image:1d5h.png|left|200px]]
[[Image:1d5h.png|left|200px]]


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{{STRUCTURE_1d5h|  PDB=1d5h  |  SCENE=  }}  
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===Rnase s(f8a). mutant ribonucleasE S.===
===Rnase s(f8a). mutant ribonucleasE S.===


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{{ABSTRACT_PUBMED_11015216}}
{{ABSTRACT_PUBMED_11015216}}


==About this Structure==
==About this Structure==
1D5H is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5H OCA].  
[[1d5h]] is a 2 chain structure of [[Ribonuclease]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5H OCA].  
 
==See Also==
*[[Ribonuclease|Ribonuclease]]


==Reference==
==Reference==
<ref group="xtra">PMID:11015216</ref><references group="xtra"/>
<ref group="xtra">PMID:011015216</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Ratnaparkhi, G S]]
[[Category: Ratnaparkhi, G S]]
[[Category: Varadarajan, R.]]
[[Category: Varadarajan, R.]]
[[Category: Hydrolase]]
[[Category: Rnase s mutant f8a cavity s protein s peptide]]
[[Category: Rnase s mutant f8a cavity s protein s peptide]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:47:48 2009''

Revision as of 13:16, 26 July 2012

File:1d5h.png


Drag the structure with the mouse to rotate
1d5h, resolution 2.25Å (default scene)
Ligands: SO4
Non-Standard Residues: SET
Related: 1rnv, 1d5d, 1d5e
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Rnase s(f8a). mutant ribonucleasE S.

Template:ABSTRACT PUBMED 11015216

About this Structure

1d5h is a 2 chain structure of Ribonuclease with sequence from Bos taurus. Full crystallographic information is available from OCA.

See Also

Reference

  1. Ratnaparkhi GS, Varadarajan R. Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics. Biochemistry. 2000 Oct 10;39(40):12365-74. PMID:11015216

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