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. Author manuscript; available in PMC: 2014 Jun 1.
Published in final edited form as: J Struct Funct Genomics. 2013 May 25;14(2):10.1007/s10969-013-9155-9. doi: 10.1007/s10969-013-9155-9

Table 3. Average minimum heavy-atom distance between “gatekeeper” residues in the channel of Hs-MIF, Gl-MIF, Pf-MIF, Pb-MIF, and Py-MIF.

Protein PDB-ID Residue 44 (X, Å) Residue 100 (X, Å)
Gl-MIF 3T5S N, 5.5 R, 3.9
Hs-MIF 1MIF Y, 5.3 V, 6.7
Pf-MIF 2WKF R, 3.6 D, 4.6
Pb-MIF 2WKB R, 5.8* D, 4.9
Py-MIF 3GAD R, 3.8 D, 4.3
*

One of the three arginine side chains in the trimer is “flipped” such that there is no three-fold symmetry between the three arginines. Consequently, the “hole” is larger at this site in Pb-MIF