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1ubq

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Revision as of 17:26, 12 November 2007 by OCA (Talk | contribs)
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Image:1ubq.gif

1ubq, resolution 1.8Å

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STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION

Overview

The crystal structure of human erythrocytic ubiquitin has been refined at, 1.8 A resolution using a restrained least-squares procedure. The, crystallographic R-factor for the final model is 0.176. Bond lengths and, bond angles in the molecule have root-mean-square deviations from ideal, values of 0.016 A and 1.5 degrees, respectively. A total of 58 water, molecules per molecule of ubiquitin are included in the final model. The, last four residues in the molecule appear to have partial occupancy or, large thermal motion. The overall structure of ubiquitin is extremely, compact and tightly hydrogen-bonded; approximately 87% of the polypeptide, chain is involved in hydrogen-bonded secondary structure. Prominent, secondary structural features include three and one-half turns of, alpha-helix, a short piece of 3(10)-helix, a mixed beta-sheet that, contains five strands, and seven reverse turns. There is a marked, hydrophobic core formed between the beta-sheet and alpha-helix. The, molecule features a number of unusual secondary structural features, including a parallel G1 beta-bulge, two reverse Asx turns, and a, symmetrical hydrogen-bonding region that involves the two helices and two, of the reverse turns.

About this Structure

1UBQ is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1UBQ with [Ubiquitin]. Full crystallographic information is available from OCA.

Reference

Structure of ubiquitin refined at 1.8 A resolution., Vijay-Kumar S, Bugg CE, Cook WJ, J Mol Biol. 1987 Apr 5;194(3):531-44. PMID:3041007

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