2ldx
CHARACTERIZATION OF THE ANTIGENIC SITES ON THE REFINED 3-ANGSTROMS RESOLUTION STRUCTURE OF MOUSE TESTICULAR LACTATE DEHYDROGENASE C4
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| , resolution 2.96Å | |||||||
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| Activity: | L-lactate dehydrogenase, with EC number 1.1.1.27 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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 StructureAbout this Structure
2LDX is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1LDX. Full crystallographic information is available from OCA.
ReferenceReference
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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