Receptor
PDB id Resolution Class Description Source Keywords
6MYD 1.4 Å EC: 2.3.2.27 STRUCTURE OF ZEBRAFISH TRAF6 IN COMPLEX WITH STING CTT DANIO RERIO INNATE IMMUNITY STING NF-KAPPAB TRAF6 TMEM173 IMMUNE SY
Ref.: MODULAR ARCHITECTURE OF THE STING C-TERMINAL TAIL A INTERFERON AND NF-KAPPA B SIGNALING ADAPTATION. CELL REP V. 27 1165 2019
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
SO4 C:601;
C:604;
C:603;
C:602;
A:601;
 Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
 none;
none;
none;
none;
none;
 submit data
96.063 O4 S [O-]S...
GLU PRO VAL GLU THR THR ASP TYR D:377;
B:377;
 Valid;
Valid;
 none;
none;
 submit data
949.945 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
6MYD 1.4 Å EC: 2.3.2.27 STRUCTURE OF ZEBRAFISH TRAF6 IN COMPLEX WITH STING CTT DANIO RERIO INNATE IMMUNITY STING NF-KAPPAB TRAF6 TMEM173 IMMUNE SY
Ref.: MODULAR ARCHITECTURE OF THE STING C-TERMINAL TAIL A INTERFERON AND NF-KAPPA B SIGNALING ADAPTATION. CELL REP V. 27 1165 2019
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 6 families.
1 6MYD - GLU PRO VAL GLU THR THR ASP TYR n/a n/a
70% Homology Family (3)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 214 families.
1 6MYD - GLU PRO VAL GLU THR THR ASP TYR n/a n/a
2 1LB6 Kd = 84 uM LYS GLN GLU PRO GLN GLU ILE ASP PHE n/a n/a
3 1LB5 - GLN MET PRO THR GLU ASP GLU TYR n/a n/a
50% Homology Family (3)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 181 families.
1 6MYD - GLU PRO VAL GLU THR THR ASP TYR n/a n/a
2 1LB6 Kd = 84 uM LYS GLN GLU PRO GLN GLU ILE ASP PHE n/a n/a
3 1LB5 - GLN MET PRO THR GLU ASP GLU TYR n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: GLU PRO VAL GLU THR THR ASP TYR; Similar ligands found: 132
No: Ligand ECFP6 Tc MDL keys Tc
1 GLU PRO VAL GLU THR THR ASP TYR 1 1
2 GLN MET PRO THR GLU ASP GLU TYR 0.654135 0.895522
3 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.591549 0.923077
4 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.574324 0.882353
5 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.558621 0.938462
6 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.543478 0.953125
7 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.517241 0.953125
8 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.513889 0.920635
9 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.506849 0.953125
10 GLU GLU ASN ASP PRO ASP TYR 0.504 0.919355
11 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.503704 0.903226
12 ACE TYR PRO ILE GLN GLU THR 0.503597 0.890625
13 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.503497 0.921875
14 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.5 0.921875
15 ILE THR ASP GLN VAL PRO PHE SER VAL 0.496644 0.892308
16 GLU ALA ASP PRO THR GLY HIS SER TYR 0.493671 0.882353
17 GLN ASN TYR PRO ILE VAL GLN 0.492857 0.921875
18 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.490446 0.808219
19 THR PRO TYR ASP ILE ASN GLN MET LEU 0.490196 0.897059
20 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.490196 0.893939
21 GLN ASN GLY PTR VAL ASN PRO THR TYR 0.489655 0.847222
22 ACE PRO VAL GLN GLU THR NH2 0.487805 0.873016
23 TYR PRO TYR 0.486726 0.825397
24 ASP ILE ASN TYR TYR THR SER GLU PRO 0.486301 0.882353
25 LEU PRO SER PHE GLU THR ALA LEU 0.486111 0.90625
26 CYS THR GLU LEU LYS LEU SER ASP TYR 0.485714 0.769231
27 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.483871 0.884058
28 ALA THR ALA ALA ALA THR GLU ALA TYR 0.483607 0.737705
29 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.483444 0.8
30 CYS THR GLU LEU LYS LEU ASN ASP TYR 0.478571 0.769231
31 TYR SEP PRO THR SEP PRO SER 0.477612 0.816901
32 SER GLU CYS THR THR PRO CYS 0.476923 0.859375
33 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.474026 0.878788
34 PHE PRO THR LYS ASP VAL ALA LEU 0.473333 0.90625
35 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.472222 0.938462
36 GLU THR HPH TYR VAL ASP 0.470588 0.701493
37 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.470149 0.918033
38 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.468966 0.953125
39 LEU PRO PHE GLU LYS SER THR VAL MET 0.467949 0.84058
40 VAL PRO LEU ARG PRO MET THR TYR 0.467532 0.810811
41 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.466667 0.9375
42 GLU THR PHE TYR VAL ASP GLY 0.466165 0.765625
43 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.459119 0.893939
44 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.458599 0.869565
45 ALA THR PRO PHE GLN GLU 0.456522 0.901639
46 LEU PHE GLY TYR PRO VAL TYR VAL 0.455782 0.876923
47 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.455782 0.938462
48 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.452703 0.909091
49 LEU PRO PHE ASP LYS THR THR ILE MET 0.452229 0.84058
50 PRO SER TYR SEP PRO THR SEP PRO SER 0.452055 0.816901
51 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.452055 0.774648
52 ACE PRO ALA PRO TYR 0.45082 0.84375
53 LYS THR PHE PRO PRO THR GLU PRO LYS 0.450331 0.920635
54 GLU VAL PTR GLU SER PRO 0.45 0.857143
55 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.449275 0.859375
56 ARG VAL SER PRO SER THR SER TYR THR PRO 0.448529 0.920635
57 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.447368 0.9375
58 ASP ARG VAL TYR 0.445378 0.68254
59 LEU PRO PHE GLU ARG ALA THR VAL MET 0.442424 0.77027
60 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.441718 0.826087
61 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.441558 0.876923
62 ASP ILE ALA TYR TYR THR SER GLU PRO 0.441379 0.895522
63 TRP GLU TYR ILE PRO ASN VAL 0.440994 0.855072
64 ALA GLU THR PHE TYR VAL ASP GLY 0.440298 0.730159
65 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.44 0.842857
66 LEU PRO PHE ASP ARG THR THR ILE MET 0.438272 0.773333
67 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.437909 0.876923
68 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.437909 0.876923
69 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.4375 0.753846
70 HIS SER ILE THR TYR LEU LEU PRO VAL 0.4375 0.857143
71 ALA GLU THR PHE 0.435897 0.672131
72 PRO THR VAL GLU GLU VAL ASP 0.435484 0.806452
73 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.434783 0.882353
74 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.434783 0.884058
75 DHI PRO PHE HIS LEU LEU VAL TYR 0.434783 0.823529
76 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.434211 0.882353
77 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.434211 0.847222
78 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.433121 0.833333
79 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.432927 0.910448
80 LEU PRO PHE ASP LYS SER THR ILE MET 0.432927 0.828571
81 SER PRO ILE VAL PRO SER PHE ASP MET 0.432258 0.828571
82 ASN ASP THR SER GLN THR SER SER PRO SER OPE 0.432258 0.777778
83 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.432099 0.897059
84 LYS PRO VAL LEU ARG THR ALA 0.431507 0.771429
85 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.431138 0.833333
86 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.430464 0.878788
87 GLN ILE MET TYR ASN TYR PRO ALA MET 0.43038 0.816901
88 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.430303 0.838235
89 ACE PRO GLN GLN ALA THR ASP ASP 0.42963 0.888889
90 THR PRO GLN ASP LEU ASN THR MET LEU 0.428571 0.850746
91 ARG THR PHE SER PRO THR TYR GLY LEU 0.428571 0.847222
92 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.426752 0.850746
93 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.425926 0.814286
94 PRO PRO ALA TYR PRO PRO PRO PRO VAL PRO 0.425532 0.904762
95 ASN ASP TRP LEU LEU PRO SER TYR 0.424242 0.871429
96 ARG ARG GLU VAL HIS THR TYR TYR 0.422078 0.726027
97 PHE ASN PHE PRO GLN ILE THR 0.421769 0.863636
98 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.421687 0.810811
99 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.420732 0.865672
100 ASP ASP ASP ASP TYR 0.419643 0.639344
101 GLY PRO THR ILE GLU GLU VAL ASP 0.419118 0.859375
102 ARG PRO MET THR TYR LYS GLY ALA LEU 0.418605 0.8
103 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.418182 0.893939
104 GLY ALA PHE THR PHE ASN GLU ASP PHE 0.41791 0.65625
105 ACE GLU VAL ASN ALA PRO VAL LPD 0.414815 0.84375
106 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.414634 0.865672
107 ASP ILE ASN TYS TYS THR SER GLU PRO 0.414474 0.722892
108 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.412162 0.71875
109 N7P THR SEP PRO SER TYR SET 0.412162 0.794521
110 ACE GLU VAL ASN PRO PRO VAL PRO NH2 0.411348 0.84375
111 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.410596 0.746479
112 ILE MET ASP GLN VAL PRO PHE SER VAL 0.409938 0.826087
113 PRO GLU ALA THR ALA PRO PRO GLU GLU 0.409722 0.875
114 LEU SER SER PRO VAL THR LYS SER PHE 0.409091 0.861538
115 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.407643 0.788732
116 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.406977 0.810811
117 GLU LEU ASP 1OL VAL GLU PHE 0.406897 0.677419
118 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.40678 0.824324
119 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.405594 0.765625
120 ACE ALA ARG THR GLU VAL TYR NH2 0.404255 0.705882
121 PRO GLU PRO THR ALA PRO PRO GLU GLU 0.40411 0.875
122 PRO GLN PTR GLU GLU ILE PRO ILE 0.403846 0.777778
123 LEU PRO PHE GLU ARG ALA THR ILE MET 0.403509 0.76
124 ASP ALA ASP GLU TYR LEU 0.401515 0.709677
125 PRO ARG GLY TYR PRO GLY GLN VAL 0.401316 0.890625
126 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.401316 0.8
127 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.401163 0.824324
128 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.4 0.865672
129 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.4 0.861538
130 GLU LEU PRO LEU VAL LYS ILE 0.4 0.769231
131 LEU PRO GLU THR GLY 0.4 0.873016
132 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.4 0.882353
Similar Ligands (3D)
Ligand no: 1; Ligand: GLU PRO VAL GLU THR THR ASP TYR; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 6MYD; Ligand: GLU PRO VAL GLU THR THR ASP TYR; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 1) in the query (biounit: 6myd.bio2) has 18 residues
No: Leader PDB Ligand Sequence Similarity
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