1bu4: Difference between revisions

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[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:24:03 2007''
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Revision as of 15:52, 30 October 2007

File:1bu4.gif


1bu4, resolution 1.9Å

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RIBONUCLEASE 1 COMPLEX WITH 2'GMP

OverviewOverview

We systematically analyzed the crystallographically determined water, molecules of all known structures of RNase T1 and compared them to the, ordered solvent in a large number of related microbial nucleases. To, assess the crystallographers' impact on the interpretation of the solvent, structure, we independently refined five validation structures from, diffraction data derived from five isomorphous crystals of RNase T1. We, also compared the positions of water molecules found in 11 published, isomorphous RNase T1 inhibitor complexes. These data suggest that the, positions of most of the waters located on the surface of a protein and, that are well-determined in the experimental electron density maps are, determined primarily by crystal packing forces. Water molecules with less, ... [(full description)]

About this StructureAbout this Structure

1BU4 is a [Single protein] structure of sequence from [Aspergillus oryzae] with CA and 2GP as [ligands]. Active as [Ribonuclease T(1)], with EC number [3.1.27.3]. Structure known Active Sites: CAL and CAT. Full crystallographic information is available from [OCA].

ReferenceReference

Conserved water molecules in a large family of microbial ribonucleases., Loris R, Langhorst U, De Vos S, Decanniere K, Bouckaert J, Maes D, Transue TR, Steyaert J, Proteins. 1999 Jul 1;36(1):117-34. PMID:10373011

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