A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN AA TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Structural highlights

1vln is a 8 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ. A Triclinic Crystal Form of the Lectin Concanavalin A J Struct Biol. 1996 Jul;117(1):16-23. PMID:8812975

1vln, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA