2ldx

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2ldx, resolution 2.96Å

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CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4

Overview

The atomic structure of mouse testicular apolactate dehydrogenase C4 has been refined to 3.0-A resolution yielding a final crystallographic R-factor of 0.256. Comparison with the refined structure of dogfish apolactate dehydrogenase A4 shows that equivalent secondary structure elements are essentially in the same position relative to the molecular 2-fold axes, except for the helices alpha D, alpha E, and alpha 2G in the vicinity of the active center, and the carboxyl-terminal helix alpha H. The positions of antigenic peptides correlate best with surface accessibilities of the monomer rather than of the full tetrameric molecule.

About this Structure

2LDX is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1LDX. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.

Reference

Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4., Hogrefe HH, Griffith JP, Rossmann MG, Goldberg E, J Biol Chem. 1987 Sep 25;262(27):13155-62. PMID:2443489

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