2cna

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2cna, resolution 2.0Å

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THE COVALENT AND THREE-DIMENSIONAL STRUCTURE OF CONCANAVALIN A, IV.ATOMIC COORDINATES,HYDROGEN BONDING,AND QUATERNARY STRUCTURE

Overview

The coordinates of the individual non-hydrogen atoms of the lectin concanavalin A have been determined from the molecular model at 2.0-A resolution and have been adjusted to make them consistent with the known stereochemistry of the constituent amino acid residues. From the coordinates, an analysis has been made of all intra- and intersubunit interactions in the molecule, yielding a description of the hydrogen-bonded structure of the monomer, including two extensive pleated sheet structures and other features of the folding of the polypeptide chain. The description of the noncovalent bonding is extended to include the interactions involved in stabilization of the dimeric and tetrameric structures of the molecule. The complete description of the molecular structure provides a basis for analysis of the biological activities of concanavalin A.

About this Structure

2CNA is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.

Reference

The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure., Reeke GN Jr, Becker JW, Edelman GM, J Biol Chem. 1975 Feb 25;250(4):1525-47. PMID:1112816

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