1phs: Difference between revisions
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[[Image:1phs.gif|left|200px]] | [[Image:1phs.gif|left|200px]] | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1phs |SIZE=350|CAPTION= <scene name='initialview01'>1phs</scene>, resolution 3.0Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PHS is a [ | 1PHS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHS OCA]. | ||
==Reference== | ==Reference== | ||
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution., Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM, EMBO J. 1990 Jan;9(1):9-15. PMID:[http:// | The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution., Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM, EMBO J. 1990 Jan;9(1):9-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2295315 2295315] | ||
[[Category: Phaseolus vulgaris]] | [[Category: Phaseolus vulgaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: plant seed storage protein (vicilin)]] | [[Category: plant seed storage protein (vicilin)]] | ||
''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 13:24:35 2008'' | ||
Revision as of 11:24, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION
Overview
The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.
About this Structure
1PHS is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution., Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM, EMBO J. 1990 Jan;9(1):9-15. PMID:2295315
Page seeded by OCA on Thu Mar 20 13:24:35 2008