1vln: Difference between revisions
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[[Image:1vln.jpg|left|200px]] | [[Image:1vln.jpg|left|200px]] | ||
'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A''' | {{Structure | ||
|PDB= 1vln |SIZE=350|CAPTION= <scene name='initialview01'>1vln</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VLN is a [ | 1VLN 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=1VLN OCA]. | ||
==Reference== | ==Reference== | ||
A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:[http:// | A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8812975 8812975] | ||
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: manganese]] | [[Category: manganese]] | ||
''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 14:47:14 2008'' | ||
Revision as of 12:47, 20 March 2008
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| 1vln, resolution 2.4Å | |||||||||||||
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| Ligands: | MN and CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A
Overview
The molecular structure of a triclinic crystal form of concanavalin A has been refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma = 97.5degrees and contain two tetramers per asymmetric unit each with approximate 222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer is more similar to that found in concanavalin A saccharide complexes than in the previously reported I222 crystal form of uncomplexed concanavalin A. A comparison of the molecular packing between the two crystal forms shows a more open arrangement with large solvent channels through the crystal.
About this Structure
1VLN is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:8812975
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