1rob: Difference between revisions
New page: left|200px<br /><applet load="1rob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rob, resolution 1.6Å" /> '''STRUCTURE OF THE CRYS... |
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[[Image:1rob.gif|left|200px]]<br /><applet load="1rob" size=" | [[Image:1rob.gif|left|200px]]<br /><applet load="1rob" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rob, resolution 1.6Å" /> | caption="1rob, resolution 1.6Å" /> | ||
'''STRUCTURE OF THE CRYSTALLINE COMPLEX OF CYTIDYLIC ACID (2'-CMP) WITH RIBONUCLEASE AT 1.6 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF THE CRYSTALLINE COMPLEX OF CYTIDYLIC ACID (2'-CMP) WITH RIBONUCLEASE AT 1.6 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The X-ray structure of the inhibitor complex of bovine ribonuclease A with | The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 A resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. A study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini. | ||
==About this Structure== | ==About this Structure== | ||
1ROB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with C2P as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http:// | 1ROB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=C2P:'>C2P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lisgarten, J | [[Category: Lisgarten, J N.]] | ||
[[Category: Palmer, R | [[Category: Palmer, R A.]] | ||
[[Category: C2P]] | [[Category: C2P]] | ||
[[Category: hydrolase(endoribonuclease)]] | [[Category: hydrolase(endoribonuclease)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:59 2008'' | ||
Revision as of 15:53, 21 February 2008
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STRUCTURE OF THE CRYSTALLINE COMPLEX OF CYTIDYLIC ACID (2'-CMP) WITH RIBONUCLEASE AT 1.6 ANGSTROMS RESOLUTION
OverviewOverview
The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 A resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. A study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini.
About this StructureAbout this Structure
1ROB is a Single protein structure of sequence from Bos taurus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures., Lisgarten JN, Gupta V, Maes D, Wyns L, Zegers I, Palmer RA, Dealwis CG, Aguilar CF, Hemmings AM, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):541-7. PMID:15299491
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