1bsr: Difference between revisions

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


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{{STRUCTURE_1bsr|  PDB=1bsr  |  SCENE=  }}  
{{STRUCTURE_1bsr|  PDB=1bsr  |  SCENE=  }}  


'''BOVINE SEMINAL RIBONUCLEASE STRUCTURE AT 1.9 ANGSTROMS RESOLUTION'''
===BOVINE SEMINAL RIBONUCLEASE STRUCTURE AT 1.9 ANGSTROMS RESOLUTION===




==Overview==
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The crystal structure of bovine seminal ribonuclease, a homodimeric enzyme closely related to pancreatic ribonuclease, has been refined at a nominal resolution of 1.9 A employing data collected on an electronic area detector. The final model consists of two chains containing 1990 non-H atoms, seven sulfate anions and 113 water molecules per asymmetric unit. The unit-cell parameters are a = 36.5 (1), b = 66.7 (1) and c = 107.5 (2) A, space group P22(1)2(1). The R factor is 0.177 for 16 492 reflections in the resolution range 6.0-1.9 A and the deviations from ideal values of bond lengths and bond angles are 0.020 A and 3.7 degrees, respectively. The molecule is formed by two pancreatic like chains, which have their N-terminal segments interchanged so that each active site is formed by residues from both subunits. The two chains are related by a non-crystallographic twofold symmetry and are covalently linked by two consecutive disulfide bridges, which form an unusual sixteen-membered ring across the dimer interface. The deviations from the molecular symmetry, the hydration shell and the sulfate-binding sites are also discussed in relation to the known structure of the pancreatic enzyme.
The line below this paragraph, {{ABSTRACT_PUBMED_15299514}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15299514}}


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mazzarella, L.]]
[[Category: Mazzarella, L.]]
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