1cjp: Difference between revisions
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[[Image:1cjp.gif|left|200px]] | [[Image:1cjp.gif|left|200px]] | ||
'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE''' | {{Structure | ||
|PDB= 1cjp |SIZE=350|CAPTION= <scene name='initialview01'>1cjp</scene>, resolution 2.78Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MUG:4-METHYLUMBELLIFERYL-ALPHA-D-GLUCOSE'>MUG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CJP is a [ | 1CJP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJP OCA]. | ||
==Reference== | ==Reference== | ||
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:[http:// | The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9087912 9087912] | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: legume lectin]] | [[Category: legume lectin]] | ||
''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 10:25:14 2008'' |
Revision as of 11:25, 20 March 2008
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, resolution 2.78Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE
OverviewOverview
Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides.
About this StructureAbout this Structure
1CJP is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:9087912
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