2sar: Difference between revisions
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|PDB= 2sar |SIZE=350|CAPTION= <scene name='initialview01'>2sar</scene>, resolution 1.8Å | |PDB= 2sar |SIZE=350|CAPTION= <scene name='initialview01'>2sar</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=3GP:GUANOSINE-3'-MONOPHOSPHATE'>3GP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sar OCA], [http://www.ebi.ac.uk/pdbsum/2sar PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2sar RCSB]</span> | |||
}} | }} | ||
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[[Category: Dodson, G G.]] | [[Category: Dodson, G G.]] | ||
[[Category: Sevcik, J.]] | [[Category: Sevcik, J.]] | ||
[[Category: hydrolase (endoribonuclease)]] | [[Category: hydrolase (endoribonuclease)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:44 2008'' |
Revision as of 05:02, 31 March 2008
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, resolution 1.8Å | |||||||
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Ligands: | , | ||||||
Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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
OverviewOverview
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 StructureAbout this Structure
2SAR is a Single protein structure of sequence from Streptomyces aureofaciens. Full crystallographic information is available from OCA.
ReferenceReference
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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