1i54 is a 2 chain structure with sequence from Thunnus thynnus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The current understanding of electron tunneling through proteins has come from work on systems where donors and acceptors are held at fixed distances and orientations. The factors that control electron flow between proteins are less well understood, owing to uncertainties in the relative orientations and structures of the reactants during the very short time that tunneling occurs. As we report here, the way around such structural ambiguity is to examine oxidation-reduction reactions in protein crystals. Accordingly, we have measured and analyzed the kinetics of electron transfer between native and Zn-substituted tuna cytochrome c (cyt c) molecules in crystals of known structure. Electron transfer rates [(320 s(-1) for *Zn-cyt c --> Fe(III)-cyt c; 2000 s(-1) for Fe(II)-cyt c --> Zn-cyt c(+))] over a Zn-Fe distance of 24.1 A closely match those for intraprotein electron tunneling over similar donor-acceptor separations. Our results indicate that van der Waals interactions and water-mediated hydrogen bonds are effective coupling elements for tunneling across a protein-protein interface.
Electron tunneling in protein crystals.,Tezcan FA, Crane BR, Winkler JR, Gray HB Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5002-6. Epub 2001 Apr 10. PMID:11296248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Tezcan FA, Crane BR, Winkler JR, Gray HB. Electron tunneling in protein crystals. Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5002-6. Epub 2001 Apr 10. PMID:11296248 doi:10.1073/pnas.081072898
