2F6B

structural and active site modification studies implicate glu, trp and arg in the activity of xylanase from alkalophilic bacillus sp. (ncl 87-6-10).

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 60
  • Norm. En. per Res.: -2.1
• Hub Node: A(1)

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
A-B	-10.4129	0.0	-115.586	-125.9989	60	3	0	4409	0	0	0

Interface residues

• A-B: ALA109A, ALA109B, ARG105A, ARG105B, ASN103A, ASN103B, ASN131A, ASN131B, ASN41A, ASN41B, ASN42A, ASN42B, ASN44A, ASN44B, ASN45A, ASN45B, ASN77A, ASN77B, ASN79A, ASN79B, ASP21B, GLN132A, GLN132B, GLN187A, GLN187B, GLY102A, GLY102B, GLY108A, GLY108B, GLY23A, GLY23B, GLY24A, GLY24B, GLY78A, GLY78B, PRO106A, PRO106B, PRO107A, PRO107B, SER188A, SER188B, SER189A, SER189B, SER22A, SER22B, THR110A, THR110B, TRP101A, TRP101B, TRP104A, TRP104B, TRP40B, TYR186A, TYR186B, TYR81A, TYR81B, VAL130A, VAL130B, VAL43A, VAL43B