1ubq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ubq.jpg|left|200px]] | + | [[Image:1ubq.jpg|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1ubq |SIZE=350|CAPTION= <scene name='initialview01'>1ubq</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1UBQ is a [ | + | 1UBQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1UBQ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb60_1.html Ubiquitin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UBQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/3041007 3041007] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: chromosomal protein]] | [[Category: chromosomal protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:29:53 2008'' |
Revision as of 12:29, 20 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION
Contents |
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.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
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 Thu Mar 20 14:29:53 2008
