1xpt

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|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene>
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene>
|LIGAND=
|LIGAND=
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xpt OCA], [http://www.ebi.ac.uk/pdbsum/1xpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xpt RCSB]</span>
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[[Category: hydrolase (phosphoric diester)]]
[[Category: hydrolase (phosphoric diester)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:12:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:56 2008''

Revision as of 21:52, 30 March 2008


PDB ID 1xpt

Drag the structure with the mouse to rotate
, resolution 1.9Å
Sites:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



BOVINE RIBONUCLEASE A (PHOSPHATE-FREE)


Overview

The structures of a new crystal form of ribonuclease A and its low-humidity variant, each containing two crystallographically independent molecules, have been determined and refined. A detailed comparison of these structures with those of the other known crystal forms of the enzyme, which have different packing arrangements and solvent composition, leads to a meaningful delineation of the rigid and flexible regions of the protein molecule and the nature of its plasticity. Many of the water molecules which are common to all the structures are involved in bridging different regions of the protein molecule, thus emphasizing the role of water in stabilizing the tertiary structure. The analysis of the structures shows that for a given N or O atom, the level of hydration increases with accessible surface area, but levels off at an area of about 10 A2. Generally, the hydration level tends to drop when the area increases beyond about 20 A2. This drop correlates with an increase in the displacement parameter. The analysis also suggests that the van der Waals radii and probe radius normally used in accessible surface area calculations are not appropriate for dealing with all situations.

About this Structure

1XPT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Plasticity, hydration and accessibility in ribonuclease A. The structure of a new crystal form and its low-humidity variant., Sadasivan C, Nagendra HG, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1343-52. PMID:10089510

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