Receptor
PDB id Resolution Class Description Source Keywords
1AQC 2.3 Å NON-ENZYME: BINDING X11 PTB DOMAIN-10MER PEPTIDE COMPLEX HOMO SAPIENS COMPLEX (PEPTIDE BINDING MODULE/PEPTIDE) PEPTIDE BINDING MODULE PTB DOMAIN
Ref.: SEQUENCE-SPECIFIC RECOGNITION OF THE INTERNALIZATION MOTIF OF THE ALZHEIMER'S AMYLOID PRECURSOR PROTEIN BY THE X11 PTB DOMAIN. EMBO J. V. 16 6141 1997
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
GLY TYR GLU ASN PRO THR TYR LYS PHE PHE C:3;
D:3;
Valid;
Valid;
none;
none;
Ki = 4.56 uM
1192.29 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1AQC 2.3 Å NON-ENZYME: BINDING X11 PTB DOMAIN-10MER PEPTIDE COMPLEX HOMO SAPIENS COMPLEX (PEPTIDE BINDING MODULE/PEPTIDE) PEPTIDE BINDING MODULE PTB DOMAIN
Ref.: SEQUENCE-SPECIFIC RECOGNITION OF THE INTERNALIZATION MOTIF OF THE ALZHEIMER'S AMYLOID PRECURSOR PROTEIN BY THE X11 PTB DOMAIN. EMBO J. V. 16 6141 1997
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 473 families.
1 1AQC Ki = 4.56 uM GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 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 355 families.
1 1AQC Ki = 4.56 uM GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 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 272 families.
1 1AQC Ki = 4.56 uM GLY TYR GLU ASN PRO THR TYR LYS PHE PHE n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: GLY TYR GLU ASN PRO THR TYR LYS PHE PHE; Similar ligands found: 163
No: Ligand ECFP6 Tc MDL keys Tc
1 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 1 1
2 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.644295 0.953846
3 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.612245 0.857143
4 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.593548 0.893939
5 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.56962 0.791667
6 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.566038 0.925373
7 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.562874 0.875
8 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.551282 0.734177
9 GLN ASN GLY PTR VAL ASN PRO THR TYR 0.54902 0.887324
10 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.548781 0.895522
11 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.545455 0.837838
12 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.542484 0.892308
13 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.530488 0.852941
14 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.524476 0.873016
15 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.522013 0.863636
16 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.515152 0.871429
17 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.512821 0.923077
18 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.508671 0.813333
19 SER SER PHE TYR PRO SEP ALA GLU GLY 0.50641 0.830986
20 SER THR SEP PRO THR PHE ASN LYS 0.506098 0.780822
21 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.505882 0.716049
22 GLN MET PRO THR GLU ASP GLU TYR 0.503145 0.869565
23 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.497175 0.893939
24 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.496815 0.787879
25 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.494118 0.783784
26 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.491124 0.925373
27 ALA GLU THR PHE TYR VAL ASP GLY 0.48951 0.71875
28 THR ASN GLU PHE TYR ALA 0.485714 0.761905
29 LEU PRO PHE GLU ARG ALA THR VAL MET 0.485549 0.727273
30 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.48503 0.865672
31 PHE SER ALA PTR PRO SER GLU GLU ASP 0.484848 0.833333
32 GLY PHE GLU PRO 0.481203 0.761905
33 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.479769 0.794521
34 VAL TYR ILE HIS PRO PHE 0.478528 0.811594
35 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.477273 0.847222
36 LEU PRO PHE GLU ARG ALA THR ILE MET 0.477273 0.717949
37 SER TYR SEP PRO THR SEP PRO SEP TYR SER 0.477124 0.777778
38 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.476471 0.833333
39 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.474026 0.723077
40 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.473988 0.895522
41 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.473373 0.805556
42 ARG VAL SER PRO SER THR SER TYR THR PRO 0.472973 0.863636
43 ASP PHE GLU ASP TYR GLU PHE ASP 0.471014 0.68254
44 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.468927 0.897059
45 LEU PHE GLY TYR PRO VAL TYR VAL 0.46875 0.863636
46 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.467066 0.882353
47 ACE TYR PRO ILE GLN GLU THR 0.464968 0.863636
48 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.464286 0.873239
49 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.463542 0.802632
50 GLU ALA ASP PRO THR GLY HIS SER TYR 0.462857 0.897059
51 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.4625 0.910448
52 GLY ASN TYR SER PHE TYR ALA LEU 0.462069 0.731343
53 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.458065 0.701493
54 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.457831 0.863636
55 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.457831 0.863636
56 PHE PRO THR LYS ASP VAL ALA LEU 0.45679 0.848485
57 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.456647 0.847222
58 ALA PRO ALA TRP LEU PHE GLU ALA 0.455621 0.768116
59 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.45509 0.865672
60 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.45509 0.84
61 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.45509 0.808219
62 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.45509 0.911765
63 LYS THR PHE PRO PRO THR GLU PRO LYS 0.454545 0.890625
64 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.452941 0.850746
65 ARG PRO MET THR TYR LYS GLY ALA LEU 0.452514 0.75641
66 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.451219 0.810811
67 LEU PRO PHE GLU LYS SER THR VAL MET 0.450292 0.777778
68 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.448864 0.794872
69 ARG ARG ARG GLU ARG SER PRO THR ARG 0.448718 0.75
70 ARG SEP PRO VAL PHE SER 0.448485 0.679487
71 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.447853 0.852941
72 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.447853 0.882353
73 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.446809 0.813333
74 ILE THR ASP GLN VAL PRO PHE SER VAL 0.446429 0.838235
75 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.44586 0.909091
76 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.444444 0.821918
77 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.44382 0.887324
78 PHE ASN PHE PRO GLN ILE THR 0.443038 0.923077
79 ARG PRO MET THR PHE LYS GLY ALA LEU 0.441341 0.717949
80 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.440994 0.731343
81 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.440476 0.787879
82 TYR PRO PHE PHE NH2 0.439716 0.84127
83 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.439024 0.835821
84 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.438202 0.897059
85 TRP GLU TYR ILE PRO ASN VAL 0.436782 0.884058
86 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.436047 0.835616
87 ARG TYR PRO LEU THR PHE GLY TRP 0.435484 0.813333
88 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.434286 0.716049
89 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.433862 0.797297
90 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.433526 0.794521
91 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.432432 0.753247
92 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.432099 0.880597
93 PRO THR SEP PRO SER TYR 0.432099 0.767123
94 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.431818 0.898551
95 GLY THR SER SER PRO SER ALA ASP 0.431507 0.830769
96 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.43038 0.742424
97 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.430233 0.69863
98 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.429379 0.826087
99 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.428571 0.686567
100 ALA VAL TYR ASN PHE ALA THR MET 0.426752 0.695652
101 THR PRO TYR ASP ILE ASN GLN MET LEU 0.426136 0.871429
102 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.425806 0.833333
103 GLY ALA PHE THR PHE ASN GLU ASP PHE 0.425676 0.714286
104 GLN ASN TYR PRO ILE VAL GLN 0.425 0.893939
105 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.424242 0.776119
106 GLY SER ASP PRO PHE LYS 0.423841 0.80303
107 MAA LYS PRO PHE 0.423611 0.707692
108 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.423077 0.911765
109 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.422222 0.746667
110 SER SER TYR ARG ARG PRO VAL GLY ILE 0.421965 0.786667
111 PRO ALA PRO PHE ALA SER ALA 0.420382 0.791045
112 GLY PHE ARG PRO 0.41958 0.7
113 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.41954 0.75
114 ASP ARG VAL TYR ILE HIS PRO PHE 0.419355 0.8
115 SER PRO THR SER PRO SEP TYR SER PRO PRO 0.419162 0.767123
116 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.418478 0.849315
117 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU 0.415584 0.863636
118 ARG PRO GLY ASN PHE PHE GLN SER ARG PRO 0.414773 0.794521
119 TYR PRO LYS ARG ILE ALA 0.414634 0.753425
120 LYS ALA VAL TYR ASN PHE ALA THR MET 0.414634 0.753623
121 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.414201 0.880597
122 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.41358 0.753425
123 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.413174 0.608108
124 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.413043 0.826087
125 HIS SER ILE THR TYR LEU LEU PRO VAL 0.412429 0.84507
126 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.412162 0.765625
127 THR TYR LYS PHE PHE GLU GLN 0.412162 0.765625
128 LEU SER SER PRO VAL THR LYS SER PHE 0.412121 0.808824
129 ARG PRO GLY ASN PHE LEU GLN SER SER PRO 0.412088 0.77027
130 LEU PRO PHE ASP LYS THR THR ILE MET 0.411429 0.788732
131 SER HIS PHE ASN GLU TYR GLU 0.411043 0.764706
132 PHE SER HIS PRO GLN ASN THR 0.410714 0.867647
133 LYS ALA LEU TYR ASN PHE ALA THR MET 0.409639 0.753623
134 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.409574 0.779221
135 LYS PRO PHE PTR VAL ASN VAL NH2 0.409357 0.833333
136 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.409357 0.865672
137 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.409091 0.779412
138 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.408805 0.676056
139 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.408284 0.880597
140 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.408284 0.848485
141 THR ASN GLU PHE TYR PHE 0.407143 0.68254
142 THR ASN GLU PHE ALA PHE 0.407143 0.619048
143 DPN PRO DAR DTH NH2 0.406667 0.742857
144 PHE ASN ARG PRO VAL 0.406452 0.760563
145 TYR SEP PRO THR SEP PRO SER 0.406452 0.780822
146 ILE SER PRO ARG THR LEU ASP ALA TRP 0.40625 0.766234
147 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.405882 0.763889
148 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.404762 0.811594
149 LEU PRO PHE ASP LYS SER THR ILE MET 0.403315 0.767123
150 ARG PHE PRO LEU THR PHE GLY TRP 0.403226 0.786667
151 PRO ALA PRO PHE ALA ALA ALA 0.402597 0.738462
152 LEU ASN PHE PRO ILE SER PRO 0.402516 0.84058
153 SER ASP ILE LEU PHE PRO ALA ASP SER 0.402439 0.808824
154 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.402367 0.743243
155 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.402174 0.76
156 GLY ALA GLU VAL PHE TYR VAL ASP GLY ALA 0.401274 0.69697
157 ASP ALA GLU PHE ARG HIS ASP SER 0.401235 0.638889
158 VAL MET ALA PRO ARG THR LEU PHE LEU 0.40113 0.705128
159 DHI PRO PHE HIS LEU LEU VAL TYR 0.401099 0.838235
160 LEU PRO PHE ASP ARG THR THR ILE MET 0.4 0.730769
161 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.4 0.815789
162 VAL PRO LEU ARG PRO MET THR TYR 0.4 0.766234
163 GLU ASN GLN LYS GLU TYR PHE PHE 0.4 0.734375
Similar Binding Sites (Proteins are less than 50% similar to leader)
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