Supporting Information

Binding Specificities of Estrogen Receptor with Perfluorinated

Compounds: A Cross Species Comparison

Zhiqiang Qiua, Kaili Qu a, Feng Luanb, Yaquan Liua, Yu Zhuc, Yongna Yuand,

Hongyu Lia, Haixia Zhange, Ying Haia, Chunyan Zhaoa*

a School of Pharmacy, Lanzhou University, Lanzhou, 730000, Chinab College of Chemistry & Chemical engineering, Yantai University, Yantai, 264005, China c Department of Ecology and Environment of Gansu Province, Lanzhou 730000, China

d School of Information Science & Engineering, Lanzhou University, Lanzhou, 730000, Chinae College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, 730000,

China

To whom correspondence should be addressed:

Chunyan Zhao,

School of Pharmacy, Lanzhou University, Lanzhou, 730000, China,

Tel.: (931) 8915686; Fax: (931) 8915686;

Email: zhaochy07@lzu.edu.cn

Figure S1. The structures of the eight PFCs.

Figure S2. The overall structural stability throughout the simulation was controlled by root-mean-

square deviations (RMSD)

Figure S3. Binding modes analysis for PFCs (PFOA, 4:2 FTOH, PFBS, PFHxS, 6:2 FTOH and

E2) to hERα and rERα. Structures of hERα and rERα are presented as ribbon. H-bonds between

residues of ERα and ligands are presented as red lines.

Figure S4. Electrostatic potentials (ESP) surface of the (A) hERα-PFCs complex and (B) rERα-

PFCs complex. The negative and positive ESPs are shown in blue and red, respectively. The H3

and H12 are presented as blue ribbon. The charge clamp residues of Lys362 and Glu542 are

presented in blue, while the residues of Asp750 and Ala743 are presented in red. The H-bonds

forming charge clamps are presented as black dot line.

Table S1. Descriptors extracted from PFCs-hERα and PFCs-rERα models.

PFCs-hERα system PFCs-rERα systemAngleNH D(D L)D（ IE）D (KE )EdgesRg AngleNH D(D L)D（ IE）D (KE )Edges Rg

PFBS 11 1 5.21 10.9619.50

80 18.49 7 1 5.24 11.1219.51 71 18.83

PFHxS 12 2 5. 17 10.8219.45 84 18.32 7 2 5.1 4 11.2119.49 72 18.33PFOS 20 3 5.18 10.7219.25 91 17.98 9 2 5.20 10.7119.46 78 18.25PFBA 10 2 5.36 10.9819.92 80 18.48 7 1 5.44 11.4219.99 62 18.5 8PFHxA10 2 5.21 10.9619.46 86 18.56 7 1 5.25 11.0819.50 65 18.45PFOA 15 3 5.19 10.8319.29 89 18.02 8 1 5.19 11.0619.41 869 18.394 :2FTOH4 1 5.24 11.0619.2 0 83 18.43 6 2 5.38 11.0819.25 69 18.306 :2 FTOH9 2 5.20 11.0419.48 84 18.41 4 2 5.21 10.9719.48 68 18.42Angle：Rotation angle of H12(°);NH: Number of H-bond between ligand and receptor (Å);D(DL): Distance

between Asp351 and Leu354 (Å); D(IE): Distance between Ile358 and Glu380 (Å);D(KE): Distance between

Lys362 and Glu542 (Å);Edges: Number of lines representing residues-residues interactions including hydrogen-bonds interaction, van der Waals force, ionization and π-π stack; Rg :Radius of gyration (Å).