2E3K

crystal structure of the human brd2 second bromodomain in complexed with the acetylated histone h4 peptide

• Total interactions analyzed: 15
• Total true interactions: 10
• Strongest Interaction:
  • Chains: C-Q
  • Int. Res.: 35
  • Norm. En. per Res.: -3.164
• Hub Node: B(4)

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	0.0	0.0	-0.0505	-0.0505	4	0	0	13	0	6	8
A-C	-27.9668	-7.7883	-177.262	-213.0171	76	5	4	7477	0	35	33
A-Q	0.0	0.0	-0.0458	-0.0458	5	0	0	23	0	0	1
B-C	-4.044	1.7458	-32.2123	-34.5105	30	7	2	1656	0	12	12
B-D	-42.4581	-1.8102	-182.188	-226.4563	81	7	4	7567	0	36	36
B-Q	-19.3219	-5.3999	-66.1651	-90.8869	29	2	0	2044	0	3	1
B-R	0.0	0.0	-0.0063	-0.0063	2	0	0	7	0	0	1
C-Q	-15.6308	2.2101	-97.3205	-110.7412	35	10	0	3368	1	6	4
D-Q	0.0	0.0	-2.3363	-2.3363	4	0	0	79	0	0	0
D-R	0.0	-3.4191	-26.1877	-29.6068	25	11	0	1119	0	5	4

Interface residues

• A-B: ARG440A, HIS384B, ILE389B, LYS441A
• A-C: ALA415A, ALA415C, ALA416A, ALA416C, ALA437A, ALA437C, ALA439C, ALA451A, ALA451C, ARG419A, ARG419C, ARG440A, ARG440C, ARG449A, ARG449C, ASN424A, ASN424C, ASN429A, ASN429C, ASP388C, ASP432A, ASP432C, ASP444A, ASP444C, ASP455A, ASP455C, CYS425A, CYS425C, GLN349A, GLN412C, GLN443A, GLN443C, GLU447A, GLU447C, HIS365A, HIS392C, HIS433C, ILE389A, ILE389C, ILE390C, LEU420A, LEU420C, LYS391C, LYS427A, LYS427C, LYS441A, LYS441C, LYS452A, LYS452C, MET453A, MET453C, PHE422A, PHE422C, PHE446A, PHE446C, PHE448A, PHE448C, PRO430A, PRO430C, PRO431A, PRO431C, PRO454A, PRO454C, SER423A, SER423C, TYR426A, TYR426C, TYR428A, TYR428C, TYR450A, TYR450C, VAL435C, VAL436A, VAL436C, VAL445A, VAL445C
• A-Q: ALA15Q, ARG3Q, GLY4Q, LYS441A, LYS452A
• B-C: ALA366C, ALA367C, ALA378B, ALA380B, ALA437C, ASP377B, ASP385B, ASP432B, ASP432C, ASP434C, ASP444C, GLY382B, HIS365C, HIS384B, HIS433B, HIS433C, LEU381B, LEU383B, LYS363C, LYS364C, LYS441C, MET438C, PRO430B, PRO431C, SER379B, TRP370C, TYR368C, TYR386B, TYR428B, VAL445C
• B-D: ALA415B, ALA415D, ALA416B, ALA416D, ALA437B, ALA437D, ALA439B, ALA439D, ALA451B, ALA451D, ARG419B, ARG419D, ARG440B, ARG440D, ARG449B, ARG449D, ASN424B, ASN424D, ASN429B, ASN429D, ASP388D, ASP432B, ASP432D, ASP444B, ASP444D, ASP455B, ASP455D, CYS425B, CYS425D, GLN349B, GLN349D, GLN412D, GLN443B, GLN443D, GLU447B, GLU447D, HIS433B, HIS433D, ILE389B, ILE389D, ILE390B, ILE390D, LEU420B, LEU420D, LYS391B, LYS391D, LYS427B, LYS427D, LYS441B, LYS441D, LYS452B, LYS452D, MET453B, MET453D, PHE422B, PHE422D, PHE446B, PHE446D, PHE448B, PHE448D, PRO430B, PRO430D, PRO431B, PRO431D, PRO454B, PRO454D, SER423B, SER423D, TYR426B, TYR426D, TYR428B, TYR428D, TYR450B, TYR450D, VAL418B, VAL418D, VAL435D, VAL436B, VAL436D, VAL445B, VAL445D
• B-Q: ALA15Q, ALA437B, ASN429B, ASP385B, ASP432B, ASP434B, CYS425B, GLY11Q, GLY13Q, GLY14Q, GLY6Q, GLY7Q, GLY9Q, HIS433B, ILE389B, LEU10Q, LEU381B, LEU383B, LYS427B, LYS8Q, MET438B, PRO430B, PRO431B, TYR386B, TYR426B, TYR428B, VAL376B, VAL435B, VAL436B
• B-R: GLY4R, LYS452B
• C-Q: ALA437C, ARG3Q, ARG440C, ASN429C, ASP385C, ASP432C, ASP434C, CYS425C, GLY11Q, GLY13Q, GLY14Q, GLY2Q, GLY382C, GLY4Q, GLY6Q, GLY7Q, GLY9Q, HIS384C, HIS433C, ILE389C, LEU10Q, LEU381C, LEU383C, LYS427C, LYS441C, LYS8Q, MET438C, PRO430C, PRO431C, SER1Q, TRP370C, TYR386C, TYR428C, VAL435C, VAL436C
• D-Q: ALA15Q, GLY14Q, LYS452D, PHE448D
• D-R: ARG3R, ASN429D, ASP385D, ASP432D, ASP434D, CYS425D, GLY382D, GLY4R, GLY6R, GLY7R, GLY9R, HIS384D, HIS433D, ILE389D, LEU381D, LEU383D, LYS427D, LYS8R, PRO430D, PRO431D, TRP370D, TYR386D, TYR428D, VAL435D, VAL436D