5ygm | pdb_00005ygm

Monomeric structure of concanavalin A at pH 7.5 from Carnivalia ensiformis

spinqualitylabelsall models 5ygm, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ygm is a 1 chain structure with sequence from Brazilian jack bean. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CONA_CANEN] D-mannose specific lectin. Publication Abstract from PubMed The structure of concanavalin A (ConA) has been studied intensively due to its specific interactions with carbohydrates and its heterometal (Ca2+ and Mn2+) coordination. Most structures from X-ray crystallography have shown ConA as a dimer or tetramer, because the complex formation requires specific crystallization conditions. Here, we reported a monomeric structure of ConA with a resolution of 1.6 A, which revealed that metal coordination could trigger sugar binding ability. The calcium coordination residue, Asn14, changes the orientation of carbohydrate binding residues and biophysical details, including structural information, providing valuable clues for the development and application of detection kits using ConA. Heterometal-coordinated monomeric concanavalin A at pH 7.5 from Canavalia ensiformis.,Chung NJ, Park YR, Lee DH, Park JH, Lee SJ J Microbiol Biotechnol. 2017 Oct 13. doi: 10.4014/jmb.1709.09057. PMID:29025256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Concanavalin A

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