1YCP
the crystal structure of fibrinogen-aa peptide 1-23 (f8y) bound to bovine thrombin explains why the mutation of phe-8 to tyrosine strongly inhibits normal cleavage at arginine-16
Total interactions analyzed 21
Total true interactions 11
Strongest Interaction Chains K-M
Int. Res. 184
Norm. En. per Res. -7.3429
Hub Node H(4)
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Weak Strong
Width of edge <-> No. of inter. res.
All Interactions
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Chains Hydro. Bond Ener. (kJ/mol) Elec. Ener. (kJ/mol) VDW. Ener. (kJ/mol) Tot. Stab. Ener. (kJ/mol) #int. res. # Short cont. #Hydr. int. #VDW pairs #salt bridges #Pot. fav. elec. int #Pot. unfav. elec. int int. res.
L-H -66.2687 -64.5125 423.532 292.7508 86 36 1 12310 9 39 27
L-K 0.0 0.0 -0.1021 -0.1021 3 0 0 29 0 2 1
H-F -54.6501 -45.4648 -213.28 -313.3949 71 21 3 8928 4 7 6
H-J 0.0 0.0 -0.0054 -0.0054 2 0 0 5 0 0 0
H-K 0.0 0.0 -0.0003 -0.0003 2 0 0 1 0 2 3
H-M 0.0 6.6621 -8.2573 -1.5952 13 0 0 341 0 9 9
J-K -45.6193 -40.4296 501.062 415.0131 61 14 1 7328 5 24 18
J-M -20.9016 -22.8675 -127.671 -171.4401 43 7 0 4736 2 13 9
K-M -267.4093 -58.1213 -1025.57 -1351.1006 184 66 29 38862 4 55 64
K-N 0.0 -2.9267 -61.4923 -64.419 35 2 2 3362 0 3 4
M-N -34.307 -58.5345 -95.8933 -188.7348 40 16 0 4496 3 5 2