3SOD

changes in crystallographic structure and thermostability of a cu,zn superoxide dismutase mutant resulting from the removal of buried cysteine

• Total interactions analyzed: 6
• Total true interactions: 4
• Strongest Interaction:
  • Chains: G-B
  • Int. Res.: 50
  • Norm. En. per Res.: -0.7944
• Hub Node: O(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
O-Y	0.0	-5.4157	-31.5429	-36.9586	48	0	3	2940	0	8	4
O-G	0.0	0.0	-0.0068	-0.0068	8	0	0	10	0	1	3
Y-G	0.0	0.0	-0.0483	-0.0483	2	0	0	16	0	0	1
G-B	0.0	-5.5353	-34.1849	-39.7202	50	1	3	2830	0	8	3

Interface residues

• O-Y: ALA150O, ALA150Y, ALA4O, ALA6O, ALA6Y, ARG113O, ARG113Y, ASN51O, ASN51Y, ASP50O, ASP50Y, GLN47O, GLN47Y, GLN53O, GLN53Y, GLY112O, GLY112Y, GLY148O, GLY148Y, GLY49O, GLY49Y, GLY54O, GLY54Y, HIS19O, HIS19Y, ILE111O, ILE111Y, ILE147O, ILE147Y, ILE149O, ILE149Y, ILE18O, LYS151O, LYS151Y, PHE48O, PHE48Y, SER57O, SER57Y, THR17O, THR17Y, THR52O, THR52Y, VAL146O, VAL146Y, VAL5O, VAL5Y, VAL7O, VAL7Y
• O-G: ASN90G, ASN90O, GLN15G, GLN15O, HIS19G, SER32O, THR30O, THR34G
• Y-G: GLN53Y, PRO13G
• G-B: ALA150B, ALA150G, ALA4B, ALA4G, ALA6B, ALA6G, ARG113B, ARG113G, ASN51B, ASN51G, ASP50B, ASP50G, GLN47B, GLN47G, GLN53B, GLN53G, GLY112B, GLY112G, GLY148B, GLY148G, GLY49B, GLY49G, GLY54B, GLY54G, HIS19B, HIS19G, ILE111B, ILE111G, ILE147B, ILE147G, ILE149B, ILE149G, ILE18B, ILE18G, LYS151B, LYS151G, PHE48B, PHE48G, SER57B, SER57G, THR17B, THR17G, THR52B, THR52G, VAL146B, VAL146G, VAL5B, VAL5G, VAL7B, VAL7G