2VQV

structure of hdac4 catalytic domain with a gain-of-function mutation bound to a hydroxamic acid inhibitor

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 89
  • Norm. En. per Res.: -0.7137
• 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	-2.4921	19.5399	-80.5628	-63.515	89	3	4	4685	0	17	10

Interface residues

• A-B: ALA35A, ALA35B, ALA74A, ALA74B, ARG154A, ARG154B, ARG37A, ARG37B, ASN119A, ASN119B, ASN225A, ASN225B, ASN82A, ASP115A, ASP115B, ASP333A, ASP333B, GLU120A, GLU120B, GLY167A, GLY167B, GLY224A, GLY224B, GLY229A, GLY229B, GLY330A, GLY331A, GLY36A, GLY36B, HIS122A, HIS198A, HIS198B, HIS295A, HIS295B, HIS34B, HIS75A, HIS75B, ILE117A, ILE117B, LEU299A, LEU299B, LEU334A, LEU334B, LEU77A, LEU77B, LEU78A, LEU78B, LEU84B, LYS20A, LYS20B, MET166A, MET166B, PHE168A, PHE168B, PHE226A, PHE226B, PHE227A, PHE227B, PRO165A, PRO165B, PRO228A, PRO228B, PRO296A, PRO296B, PRO298A, PRO298B, PRO83A, PRO83B, SER123B, SER163A, SER163B, THR116A, THR116B, THR164A, THR164B, THR297A, THR297B, THR81A, THR81B, TRP118A, TRP118B, TYR170A, TYR170B, TYR332A, TYR332B, TYR79A, TYR79B, VAL121A, VAL121B