Stability and Mutations Click the buttons to change the display
Cartoon view shows subunit Nqo2 in red colore with the disulfide bond between the residues Cys144 in the last beta strand and Cys172 in the loop, both are in spacefilling view and cpk color, this bonding found to cause the high stability for this subunit.

Trace view for Subunit 6 which contains the N2 cluster in cpk view with purple color which is coordinated by Cys residues as showing in the structure in spacefilling view and red color. Cys45 and Cys46 are too close to each other comparing with others Cys.

This view shows the cluster N2 forms H-bonds with Arg84 and His169,which are both from subunit Nqo4. Mutations of these 2 residues have reported as reason for the unability to detect cluster N2.


Leonid A. Sazanov, Philip Hinchliffe
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus.
Science 2006, 311: 1430-1436 (PubMed)

2FUG (PDB)

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