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. 2015 May 14;71(Pt 6):1295–1306. doi: 10.1107/S1399004715005817

Figure 5.

Figure 5

Hb quaternary features of the IsdHN2N3–metHb complex (PDB entry 4xs0; yellow), O2-ligated R-state Hb (PDB entry 2dn1; red), deoxy T-state Hb (PDB entry 2dn2; blue), CO-ligated ζ2β2 S (PDB entry 3w4u; cyan) and cat metHb (PDB entry 3gqp; green). (a) Detail of the switch region of the α1β2 interface, showing the relative positions of the α1 subunit helix C and the β2 subunit FG corner. (b) Detail of the joint region of the α1β2 interface, showing the relative positions of the β2 helix C and the α1 FG corner. In the R and T states the side chain of β2Trp37 contacts the side chain of α1Pro95. In the IsdHN2N3–metHb complex, the side chain of α1Arg92 separates β2Trp37 and α1Pro95 and makes salt bridges with α1Asp94 and the terminal carboxyl of the α1 subunit (van der Waals contacts are represented by dashed green lines; hydrogen-bonding interactions are represented by dashed magenta lines). (c) Comparison of the joint region of the α1β2 interface from IsdHN2N3–metHb, ζ2β2 S and cat metHb.