Receptor
PDB id Resolution Class Description Source Keywords
3CYY 2.4 Å NON-ENZYME: OTHER THE CRYSTAL STRUCTURE OF ZO-1 PDZ2 IN COMPLEX WITH THE CX43 HOMO SAPIENS PROTEIN-LIGAND COMPLEX CELL JUNCTION MEMBRANE PHOSPHOPROTDOMAIN TIGHT JUNCTION GAP JUNCTION TRANSMEMBRANE PEPTIDPROTEIN
Ref.: DOMAIN-SWAPPED DIMERIZATION OF ZO-1 PDZ2 GENERATES AND REGULATORY CONNEXIN43-BINDING SITES EMBO J. V. 27 2113 2008
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ARG PRO ARG PRO ASP ASP LEU GLU ILE C:1;
D:1;
Valid;
Valid;
none;
none;
Kd = 16.8 uM
1109.23 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
3CYY 2.4 Å NON-ENZYME: OTHER THE CRYSTAL STRUCTURE OF ZO-1 PDZ2 IN COMPLEX WITH THE CX43 HOMO SAPIENS PROTEIN-LIGAND COMPLEX CELL JUNCTION MEMBRANE PHOSPHOPROTDOMAIN TIGHT JUNCTION GAP JUNCTION TRANSMEMBRANE PEPTIDPROTEIN
Ref.: DOMAIN-SWAPPED DIMERIZATION OF ZO-1 PDZ2 GENERATES AND REGULATORY CONNEXIN43-BINDING SITES EMBO J. V. 27 2113 2008
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1256 families.
1 3CYY Kd = 16.8 uM ARG PRO ARG PRO ASP ASP LEU GLU ILE n/a n/a
70% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1068 families.
1 3CYY Kd = 16.8 uM ARG PRO ARG PRO ASP ASP LEU GLU ILE n/a n/a
50% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 922 families.
1 3CYY Kd = 16.8 uM ARG PRO ARG PRO ASP ASP LEU GLU ILE n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ARG PRO ARG PRO ASP ASP LEU GLU ILE; Similar ligands found: 141
No: Ligand ECFP6 Tc MDL keys Tc
1 ARG PRO ARG PRO ASP ASP LEU GLU ILE 1 1
2 LEU PRO PRO GLU GLU ARG LEU ILE 0.583333 0.968254
3 ARG PRO LYS ARG ILE ALA 0.573643 0.936508
4 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.567376 0.910448
5 ARG PRO LYS PRO LEU VAL ASP PRO 0.559055 0.920635
6 LYS PRO VAL LEU ARG THR ALA 0.521739 0.880597
7 ASN ARG PRO ILE LEU SER LEU 0.521739 0.897059
8 GLU LEU PRO LEU VAL LYS ILE 0.514925 0.825397
9 SER PRO LYS ARG ILE ALA 0.511111 0.893939
10 SER ALA PRO ASP THR ARG PRO ALA 0.507143 0.869565
11 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.506944 0.909091
12 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.503268 0.925373
13 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.503067 0.873239
14 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.5 0.882353
15 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.5 0.869565
16 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.496774 0.867647
17 ALA PRO ASP THR ARG PRO 0.496296 0.882353
18 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.493421 0.815385
19 LEU PRO PHE ASP ARG THR THR ILE MET 0.490566 0.849315
20 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.489796 0.857143
21 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.483871 0.761905
22 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.477987 0.939394
23 SER PRO LEU ASP SER LEU TRP TRP ILE 0.477124 0.767123
24 ARG ARG ARG GLU ARG SER PRO THR ARG 0.475524 0.852941
25 THR LYS PRO ARG 0.475 0.84127
26 DPN PRO DAR ILE NH2 0.473684 0.846154
27 SER HIS PRO ARG PRO ILE ARG VAL 0.473684 0.885714
28 PHE ASN ARG PRO VAL 0.471014 0.865672
29 ARG PRO PRO LYS PRO ARG PRO ARG 0.470588 0.84127
30 LEU PRO PHE GLU ARG ALA THR ILE MET 0.467066 0.835616
31 TYR PRO LYS ARG ILE ALA 0.466216 0.855072
32 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.465753 0.910448
33 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.462025 0.859155
34 LEU ASP PRO ARG 0.461538 0.920635
35 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.459459 0.73913
36 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.458599 0.909091
37 ACE GLN GLU ARG GLU VAL PRO CYS 0.458333 0.892308
38 GLU ARG THR ILE PRO ILE THR ARG GLU 0.458333 0.910448
39 ARG PRO GLY ASN PHE LEU GLN SER SER PRO 0.457831 0.871429
40 ILE SER PRO ARG THR LEU ASP ALA TRP 0.457143 0.863014
41 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.456954 0.857143
42 ALA MET ALA PRO ARG THR LEU LEU LEU 0.455782 0.819444
43 5JP PRO LYS ARG ILE ALA 0.454545 0.867647
44 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.450867 0.805195
45 LEU PRO GLU THR GLY 0.449612 0.776119
46 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.448276 0.852941
47 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.447205 0.842857
48 VAL PRO LEU ARG PRO MET THR TYR 0.446541 0.813333
49 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.44586 0.869565
50 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.445783 0.837838
51 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.444444 0.782609
52 ALA PRO ASP THR ARG PRO ALA PRO 0.443662 0.882353
53 LEU PRO GLY GLU GLU ASP LEU PRO GLY 0.442857 0.873016
54 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.442177 0.882353
55 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.442177 0.893939
56 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL 0.442029 0.920635
57 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.441379 0.835821
58 VAL PRO PRO PRO ARG PRO PRO PRO PRO GLU 0.441176 0.890625
59 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.440994 0.835616
60 LEU PRO PHE GLU ARG ALA THR VAL MET 0.440476 0.821918
61 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.439024 0.859155
62 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.43871 0.810811
63 PRO VAL LYS ARG ARG LEU ASP LEU GLU 0.438356 0.873016
64 ALA PRO ASP THR ARG PRO A2G 0.438272 0.789474
65 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.438272 0.84507
66 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.438272 0.833333
67 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.436782 0.871429
68 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.436709 0.884058
69 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.436047 0.885714
70 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.435065 0.910448
71 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.434524 0.767123
72 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.434524 0.871429
73 ARG ARG ALA SEP ALA PRO LEU PRO 0.434211 0.833333
74 SER ASP ILE LEU PHE PRO ALA ASP SER 0.433333 0.782609
75 ARG SER ALA SEP GLU PRO SER LEU 0.433121 0.835616
76 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.432099 0.760563
77 SER LEU ILE PRO TPO PRO ASP LYS 0.431373 0.77027
78 ALA PRO ASP SER ARG PRO A2G 0.43125 0.789474
79 ASP LEU THR ARG PRO 0.430657 0.895522
80 DPN PRO DAR DTH NH2 0.430657 0.794118
81 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.426752 0.867647
82 GLU PTR LEU GLY LEU ASP VAL PRO VAL 0.425197 0.809524
83 GLU PRO GLY GLY SER ARG 0.42446 0.835821
84 LEU PRO PHE ASP LYS THR THR ILE MET 0.423313 0.739726
85 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.422222 0.794872
86 3BY PRO LYS ARG ILE ALA 0.421769 0.895522
87 SER GLN LEU LYS ASN ASN ALA LYS GLU ILE 0.421429 0.661765
88 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.421053 0.859155
89 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.420382 0.768116
90 CYS THR PRO SER ARG 0.42029 0.811594
91 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.420118 0.813333
92 ALA PRO ASP CYS ARG PRO A2G 0.419753 0.769231
93 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.41958 0.710145
94 SER ARG ASP HIS SER ARG THR PRO MET 0.419162 0.813333
95 PRO SER ILE ASP ARG SER THR LYS PRO 0.41875 0.911765
96 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.41875 0.670732
97 PRO PRO LYS ARG ILE ALA 0.417808 0.936508
98 ARG THR PRO SEP LEU PRO THR 0.417219 0.821918
99 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.416667 0.84507
100 ARG PRO MET THR TYR LYS GLY ALA LEU 0.416185 0.802632
101 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.416149 0.859155
102 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.416058 0.716418
103 THR PRO GLN ASP LEU ASN THR MET LEU 0.415584 0.75
104 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.413793 0.821918
105 SER PRO HIS ASN PRO ILE SER ASP VAL ASP 0.413043 0.823529
106 ACE ARG THR PRO SEP LEU PRO THR PIP 0.412903 0.779221
107 ARG PRO MET THR PHE LYS GLY ALA LEU 0.412791 0.810811
108 SER PRO ARG LEU PRO LEU LEU GLU SER 0.412587 0.904762
109 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.4125 0.797297
110 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.411765 0.779412
111 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.410811 0.78481
112 PHE ASN PHE PRO GLN ILE THR 0.410596 0.736111
113 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.409938 0.732394
114 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.409938 0.785714
115 DTY ILE ARG LEU LPD 0.409396 0.84058
116 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.409091 0.71831
117 NGA ALA PRO ASP THR ARG PRO ALA PRO 0.409091 0.789474
118 ALA PRO ASP THR ARG PRO ALA PRO NGA 0.409091 0.789474
119 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.408805 0.924242
120 GLN MET PRO THR GLU ASP GLU TYR 0.408805 0.72
121 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.408284 0.75
122 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.408046 0.885714
123 SER MET PRO GLU LEU SER PRO VAL LEU 0.407895 0.774648
124 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.407643 0.847222
125 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.407643 0.811594
126 ALA PRO PRO PRO ARG PRO PRO LYS PRO 0.407143 0.84375
127 ASP ARG VAL TYR ILE HIS PRO PHE 0.40678 0.849315
128 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.406452 0.880597
129 ARG GLU ARG SER PRO THR ARG 0.406015 0.863636
130 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.405714 0.824324
131 ALA ARG LYS ILE ASP ASN LEU ASP 0.405594 0.784615
132 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.404494 0.826667
133 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.404255 0.78481
134 VAL MET ALA PRO ARG THR LEU PHE LEU 0.403614 0.797297
135 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.403509 0.794872
136 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.403509 0.788732
137 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.402597 0.710145
138 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.402367 0.767123
139 SER ARG LYS ILE ASP ASN LEU ASP 0.401361 0.75
140 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.4 0.75
141 LYS PRO SEP GLN GLU LEU 0.4 0.75
Similar Binding Sites (Proteins are less than 50% similar to leader)
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