1cjp
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1cjp |SIZE=350|CAPTION= <scene name='initialview01'>1cjp</scene>, resolution 2.78Å | |PDB= 1cjp |SIZE=350|CAPTION= <scene name='initialview01'>1cjp</scene>, resolution 2.78Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MUG:4-METHYLUMBELLIFERYL-ALPHA-D-GLUCOSE'>MUG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjp OCA], [http://www.ebi.ac.uk/pdbsum/1cjp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cjp RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Kanellopoulos, P N.]] | [[Category: Kanellopoulos, P N.]] | ||
[[Category: Tucker, P A.]] | [[Category: Tucker, P A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: MUG]] | ||
[[Category: legume lectin]] | [[Category: legume lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:22:56 2008'' |
Revision as of 16:22, 30 March 2008
| |||||||
| , resolution 2.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE
Overview
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 Structure
1CJP is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
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:9087912
Page seeded by OCA on Sun Mar 30 19:22:56 2008
