Close-up stereo view of the active site. Hydrogen-bonds (<4.0 Å) between Nb-GSH and the enzyme are shown as dashed lines.

Katholiki Skopelitou (173273)
Prathusha Dhavala (173280)
Anastassios C. Papageorgiou (173288)
Nikolaos E. Labrou (173294)

Publication date

April 2012

DOI

10.1371/journal.pone.0034263.g004

Abstract

<p>W304 and W117 from the proposed electron-sharing network are depicted. The orientation of Nb-GSH is the same as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0034263#pone-0034263-g003" target="_blank">Figure 3C</a>. The figure was produced using the CCP4 molecular graphics program <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0034263#pone.0034263-Pterton1" target="_blank">[56]</a>.</p

Extracted data

We use cookies to provide a better user experience.

Data Protection

Close-up stereo view of the active site. Hydrogen-bonds (<4.0 Å) between Nb-GSH and the enzyme are shown as dashed lines.

Abstract

Extracted data

Close-up stereo view of the active site. Hydrogen-bonds (<4.0 Å) between Nb-GSH and the enzyme are shown as dashed lines.

Abstract

Extracted data

Related items

Related items