1URD

x-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium alicyclobacillus acidocaldarius provide insight into acid stability of proteins

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 83
  • Norm. En. per Res.: -0.6294
• 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	-8.4995	-9.3723	-34.3692	-52.241	83	1	4	3215	1	17	23

Interface residues

• A-B: ALA238A, ALA240A, ALA240B, ALA244A, ALA244B, ALA263B, ALA50B, ALA51B, ALA54B, ASN234A, ASN234B, ASN69A, ASN69B, ASP259B, ASP59B, ASP65A, ASP65B, GLN38A, GLN44A, GLN44B, GLN48A, GLN66A, GLN66B, GLU241A, GLU241B, GLY245B, GLY40A, ILE237A, ILE237B, ILE265B, ILE62A, ILE62B, LEU243A, LEU243B, LEU43A, LEU43B, LYS239A, LYS246A, LYS246B, LYS262A, LYS262B, LYS264B, LYS379A, LYS47A, LYS47B, LYS55B, LYS60A, LYS60B, LYS71A, LYS84A, LYS84B, MET172A, PHE75A, PRO41B, PRO70A, PRO70B, PRO86A, SER232A, SER232B, SER236A, SER236B, SER36A, SER67A, SER67B, SER68A, SER68B, THR230A, THR230B, THR233A, THR233B, THR31A, THR31B, THR33A, THR33B, THR39A, THR39B, TRP35A, TRP35B, VAL61B, VAL63A, VAL63B, VAL64A, VAL64B