2sar
From Proteopedia
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| - | [[Image:2sar.jpg|left|200px]] | + | [[Image:2sar.jpg|left|200px]] |
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| - | '''DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2sar |SIZE=350|CAPTION= <scene name='initialview01'>2sar</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=3GP:GUANOSINE-3'-MONOPHOSPHATE'>3GP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SAR is a [ | + | 2SAR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SAR OCA]. |
==Reference== | ==Reference== | ||
| - | Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8 A resolution., Sevcik J, Dodson EJ, Dodson GG, Acta Crystallogr B. 1991 Apr 1;47 ( Pt 2):240-53. PMID:[http:// | + | Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8 A resolution., Sevcik J, Dodson EJ, Dodson GG, Acta Crystallogr B. 1991 Apr 1;47 ( Pt 2):240-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1654932 1654932] |
[[Category: Ribonuclease T(1)]] | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase (endoribonuclease)]] | [[Category: hydrolase (endoribonuclease)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:09 2008'' |
Revision as of 16:38, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DETERMINATION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURES OF RIBONUCLEASE SA AND ITS COMPLEX WITH 3'-GUANYLIC ACID AT 1.8 ANGSTROMS RESOLUTION
Overview
The crystal structures of ribonuclease from Streptomyces aureofaciens (RNase Sa) and its complex with 3'-guanylic acid (guanosine 3'-monophosphate, 3'-GMP) have been determined by the method of isomorphous replacement. The atomic parameters have been refined by restrained least-squares minimization using data in the resolution range 10.0-1.8 A. All protein atoms and more than 230 water atoms in the two crystal structures have been refined to crystallographic R factors of 0.172 and 0.175 respectively. The estimated r.m.s. error in the atomic positions ranges from 0.2 A for well-defined atoms to about 0.5 A for more poorly defined atoms. There are two enzyme molecules in the asymmetric unit, built independently, and referred to as molecules A and B. The value of the average B factor for protein atoms in both structures is about 19 A2 and for water molecules about 35 A2. Electron density for the substrate analogue 3'-GMP was found only at the active site of molecule A. The density was very clear and the positions of all 3'-GMP atoms were refined with precision comparable to that of the protein.
About this Structure
2SAR is a Single protein structure of sequence from Streptomyces aureofaciens. Full crystallographic information is available from OCA.
Reference
Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8 A resolution., Sevcik J, Dodson EJ, Dodson GG, Acta Crystallogr B. 1991 Apr 1;47 ( Pt 2):240-53. PMID:1654932
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