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1vln
From Proteopedia
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| - | [[Image:1vln.jpg|left|200px]] | + | [[Image:1vln.jpg|left|200px]] |
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| - | '''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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| , resolution 2.4Å | |||||||
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| Ligands: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 14:47:14 2008
Categories: Canavalia ensiformis | Single protein | Hamodrakas, S J. | Kanellopoulos, P N. | Tucker, P A. | CA | MN | Calcium | Lectin | Legume | Manganese
