3OLM

structure and function of a ubiquitin binding site within the catalytic domain of a hect ubiquitin ligase

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-D
  • Int. Res.: 74
  • Norm. En. per Res.: -3.2986
• 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-D	-19.9447	-6.4018	-217.747	-244.0935	74	8	7	8570	0	21	11

Interface residues

• A-D: ALA46D, ALA523A, ARG42D, ARG617A, ARG72D, ARG74D, ASN463A, ASN513A, ASN532A, ASN534A, ASN538A, ASN543A, ASP39D, CYS517A, GLN40D, GLN41D, GLN470A, GLN49D, GLU34D, GLU466A, GLU510A, GLU520A, GLU540A, GLU616A, GLU620A, GLY10D, GLY47D, GLY536A, GLY619A, HIS541A, HIS68D, ILE13D, ILE30D, ILE36D, ILE44D, ILE537A, ILE548A, LEU43D, LEU50D, LEU518A, LEU542A, LEU67D, LEU69D, LEU71D, LEU73D, LEU8D, LYS11D, LYS48D, LYS6D, PHE45D, PHE465A, PHE512A, PHE515A, PHE519A, PHE545A, PHE618A, PRO37D, PRO514A, PRO539A, SER535A, THR12D, THR66D, THR7D, THR9D, TYR469A, TYR516A, TYR521A, TYR524A, TYR527A, TYR544A, VAL5D, VAL621A, VAL622A, VAL70D