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1ubq

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ubq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ubq OCA], [http://www.ebi.ac.uk/pdbsum/1ubq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ubq RCSB]</span>
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'''STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION'''
'''STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION'''
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[[Category: Cook, W J.]]
[[Category: Cook, W J.]]
[[Category: Vijay-Kumar, S.]]
[[Category: Vijay-Kumar, S.]]
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[[Category: chromosomal protein]]
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[[Category: Chromosomal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:00:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:04 2008''
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Revision as of 08:00, 3 May 2008

Image:1ubq.jpg


PDB ID 1ubq

Drag the structure with the mouse to rotate
1ubq, resolution 1.80Å ()
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 Page seeded by OCA on Sat May 3 11:00:46 2008

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