1nxd: Difference between revisions

Revision as of 09:04, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nxd.png

Template:STRUCTURE 1nxd

Crystal structure of MnMn Concanavalin ACrystal structure of MnMn Concanavalin A

Template:ABSTRACT PUBMED 15159564

About this StructureAbout this Structure

1NXD is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

ReferenceReference

Structure of concanavalin A at pH 8: bound solvent and crystal contacts., Lopez-Jaramillo FJ, Gonzalez-Ramirez LA, Albert A, Santoyo-Gonzalez F, Vargas-Berenguel A, Otalora F, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1048-56. Epub 2004, May 21. PMID:15159564

Page seeded by OCA on Tue Jul 29 09:04:00 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nxd.gif|left|200px]]
+{{Seed}}
+[[Image:1nxd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nxd|  PDB=1nxd  |  SCENE=  }}
-'''Crystal structure of MnMn Concanavalin A'''
+===Crystal structure of MnMn Concanavalin A===
-==Overview==
+<!--
-Concanavalin A has been crystallized in the presence of the ligand (6-S-beta-D-galactopyranosyl-6-thio)-cyclomaltoheptaose. The crystals are isomorphous to those reported for ConA complexed with peptides at low resolution (3.00-2.75 angstroms). The structure was solved at 1.9 angstroms, with free R and R values of 0.201 and 0.184, respectively. As expected, no molecules of the ligand were bound to the protein. Soaking in the cryobuffer left its fingerprint as 25 molecules of glycerol in the bound solvent, most of them at specific positions. The fact that a glycerol molecule is located in the sugar-binding pocket of each of the four subunits in the asymmetric unit and another is located in two of the peptide-binding sites suggests a recognition phenomenon rather than a displacement of water molecules by glycerol. Crystal contact analysis shows that a relation exists between the residues that form hydrogen bonds to other asymmetric units and the space group: contact Asp58-Ser62 is a universal feature of ConA crystals, while Ser66-His121, Asn69-Asn118 and Tyr100-His205 contacts are general features of the C222(1) crystal form.
+The line below this paragraph, {{ABSTRACT_PUBMED_15159564}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15159564 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15159564}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Vargas-Berenguel, A.]]
 [[Category: Lectin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:05:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:04:00 2008''