8KME

crystal structure of human alpha-thrombin inhibited with sel2770.

• Total interactions analyzed: 6
• Total true interactions: 3
• Strongest Interaction:
  • Chains: 2-3
  • Int. Res.: 36
  • Norm. En. per Res.: -2.92
• Hub Node: 2(2)

All Interactions

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
1-2	-71.112	-57.4731	361.561	232.9759	84	41	1	13194	7	38	28
2-3	0.0	-1.1129	-104.008	-105.1209	36	1	2	4464	1	10	4
2-4	0.0	0.0	-12.0707	-12.0707	17	1	0	1060	0	0	0

Interface residues

• 1-2: ALA11, ALA1322, ALA222, ARG1372, ARG141, ARG2062, ARG41, ASN1592, ASN2042, ASN2052, ASP11, ASP1162, ASP119, ASP141, ASP212, ASP492, CB8.12981-44.08750, CYS11, CYS1222, GLN1312, GLN2092, GLU131, GLU141, GLU232, GLU81, GLY1332, GLY1362, GLY21, GLY252, HIS1192, ILE1182, ILE1622, ILE242, ILE472, LEU121, LEU1232, LEU1292, LEU1302, LEU141, LEU1602, LEU31, LEU462, LEU61, LYS101, LYS1352, LYS141, LYS1862, LYS2022, LYS91, MET2012, MET2102, MET262, PHE1142, PHE1992, PHE2042, PHE71, PRO1202, PRO1242, PRO1612, PRO2042, PRO282, PRO51, SER111, SER1152, SER1292, SER141, SER202, SER2032, SER272, SER482, THR1392, THR141, TRP2072, TRP292, TYR1172, TYR1342, TYR141, TYR1842, TYR2082, VAL1212, VAL1382, VAL1572, VAL1582, VAL2002
• 2-3: ARG352, ARG672, ARG732, ARG752, ARG772, ASN622, ASP3553, ASP632, GLN1512, GLN382, GLU3573, GLU3583, GLU3613, GLU3623, GLU392, GLU772, GLU802, ILE3593, ILE822, LEU3643, LEU402, LEU412, LEU652, LYS362, LYS702, MET322, MET842, PHE342, PHE3563, PRO3603, PRO372, SER362, SER722, THR742, TRP1412, TYR762
• 2-4: ARG1732, ARG1752, ARG2212, ARG972, ASN982, GLU2172, GLU972, GLY2162, GLY2192, ILE1742, LEU3904, LYS2242, PRO3914, SER1712, THR1722, TRP2152, TYR602